DELTA-G
comment: For biochemical reactions, this property refers to the standard transformed Gibbs energy change for a reaction written in terms of biochemical reactants (sums of species), delta-G'o. delta-G'o = -RT lnK' and delta-G'o = delta-H'o - T delta-S'o delta-G'o has units of kJ/mol. Like K', it is a function of temperature (T), ionic strength (I), pH, and pMg (pMg = -log10[Mg2+]). Therefore, these quantities must be specified, and values for DELTA-G for biochemical reactions are represented as 5-tuples of the form (delta-G'o T I pH pMg). This property may have multiple values, representing different measurements for delta-G'o obtained under the different experimental conditions listed in the 5-tuple. (This definition from EcoCyc)
type: ObjectProperty
domain: biochemicalReaction
range: deltaGprimeO

CELLTYPE
type: ObjectProperty
comment: A cell type, e.g. 'HeLa'. This should reference a term in a controlled vocabulary of cell types.
domain: bioSource
range: openControlledVocabulary

CELLULAR-LOCATION
type: ObjectProperty
comment: A cellular location, e.g. 'cytoplasm'. This should reference a term in the Gene Ontology Cellular Component ontology. The location referred to by this property should be as specific as is known. If an interaction is known to occur in multiple locations, separate interactions (and physicalEntityParticipants) must be created for each different location. Note: If a location is unknown then the GO term for 'cellular component unknown' (GO:0008372) should be used in the LOCATION property. If the location of a participant in a complex is unspecified, it may be assumed to be the same location as that of the complex. In case of conflicting information, the location of the most outer layer of any nesting should be considered correct. Note: Cellular location describes a specific location of a physical entity as it would be used in e.g. a transport reaction. It does not describe all of the possible locations that the physical entity could be in the cell.
range: openControlledVocabulary
domain: physicalEntityParticipant

COFACTOR
type: ObjectProperty
comment: Any cofactor(s) or coenzyme(s) required for catalysis of the conversion by the enzyme. COFACTOR is a sub-property of PARTICIPANTS.
sub property of: PARTICIPANTS
domain: catalysis
range: physicalEntityParticipant

COMPONENTS
type: ObjectProperty
comment: Defines the physicalEntity subunits of this complex. This property should not contain other complexes, i.e. it should always be a flat representation of the complex. For example, if two protein complexes join to form a single larger complex via a complex assembly interaction, the COMPONENTS of the new complex should be the individual proteins of the smaller complexes, not the two smaller complexes themselves. Exceptions are black-box complexes (i.e. complexes in which the COMPONENTS property is empty), which may be used as COMPONENTS of other complexes (via a physicalEntityParticipant instance) because their constituent parts are unknown / unspecified. The reason for keeping complexes flat is to signify that there is no information stored in the way complexes are nested, such as assembly order.
domain: complex
range: physicalEntityParticipant

CONFIDENCE
type: ObjectProperty
comment: Confidence in the containing instance. Usually a statistical measure.
range: confidence
domain: evidence

CONTROLLED
type: ObjectProperty
comment: The entity that is controlled, e.g., in a biochemical reaction, the reaction is controlled by an enzyme. CONTROLLED is a sub-property of PARTICIPANTS.
sub property of: PARTICIPANTS
domain: control
range: Class
  union of: interaction
  union of: pathway

CONTROLLER
type: ObjectProperty
comment: The controlling entity, e.g., in a biochemical reaction, an enzyme is the controlling entity of the reaction. CONTROLLER is a sub-property of PARTICIPANTS.
sub property of: PARTICIPANTS
domain: control
range: physicalEntityParticipant

DATA-SOURCE
type: ObjectProperty
comment: A free text description of the source of this data, e.g. a database or person name. This property should be used to describe the source of the data. This is meant to be used by databases that export their data to the BioPAX format or by systems that are integrating data from multiple sources. The granularity of use (specifying the data source in many or few instances) is up to the user. It is intended that this property report the last data source, not all data sources that the data has passed through from creation.
range: dataSource
domain: entity

EVIDENCE
type: ObjectProperty
comment: Scientific evidence supporting the existence of the entity as described.
range: evidence
domain: Class
  union of: interaction
  union of: pathway

EVIDENCE-CODE
type: ObjectProperty
comment: A pointer to a term in an external controlled vocabulary, such as the GO, PSI-MI or BioCyc evidence codes, that describes the nature of the support, such as 'traceable author statement' or 'yeast two-hybrid'.
domain: evidence
range: openControlledVocabulary

EXPERIMENTAL-FORM
type: ObjectProperty
comment: The experimental forms associated with an evidence instance.
domain: evidence
range: experimentalForm

EXPERIMENTAL-FORM-TYPE
type: ObjectProperty
comment: Descriptor of this experimental form from a controlled vocabulary.
domain: experimentalForm
range: openControlledVocabulary

FEATURE-LOCATION
type: ObjectProperty
comment: Location of the feature on the sequence of the interactor. One feature may have more than one location, used e.g. for features which involve sequence positions close in the folded, three-dimensional state of a protein, but non-continuous along the sequence.
domain: sequenceFeature
range: sequenceLocation

FEATURE-TYPE
type: ObjectProperty
comment: Description and classification of the feature.
range: openControlledVocabulary
domain: sequenceFeature

INTERACTION-TYPE
type: ObjectProperty
comment: External controlled vocabulary characterizing the interaction type, for example "phosphorylation".
range: openControlledVocabulary
domain: physicalInteraction

KEQ
type: ObjectProperty
comment: This quantity is dimensionless and is usually a single number. The measured equilibrium constant for a biochemical reaction, encoded by the slot KEQ, is actually the apparent equilibrium constant, K'. Concentrations in the equilibrium constant equation refer to the total concentrations of all forms of particular biochemical reactants. For example, in the equilibrium constant equation for the biochemical reaction in which ATP is hydrolyzed to ADP and inorganic phosphate: K' = [ADP][Pi]/[ATP], The concentration of ATP refers to the total concentration of all of the following species: [ATP] = [ATP4-] + [HATP3-] + [H2ATP2-] + [MgATP2-] + [MgHATP-] + [Mg2ATP]. The apparent equilibrium constant is formally dimensionless, and can be kept so by inclusion of as many of the terms (1 mol/dm3) in the numerator or denominator as necessary. It is a function of temperature (T), ionic strength (I), pH, and pMg (pMg = -log10[Mg2+]). Therefore, these quantities must be specified to be precise, and values for KEQ for biochemical reactions may be represented as 5-tuples of the form (K' T I pH pMg). This property may have multiple values, representing different measurements for K' obtained under the different experimental conditions listed in the 5-tuple. (This definition adapted from EcoCyc)
domain: biochemicalReaction
range: kPrime

LEFT
type: ObjectProperty
comment: The participants on the left side of the conversion interaction. Since conversion interactions may proceed in either the left-to-right or right-to-left direction, occupants of the LEFT property may be either reactants or products. LEFT is a sub-property of PARTICIPANTS.
sub property of: PARTICIPANTS
domain: conversion
range: physicalEntityParticipant

NEXT-STEP
type: ObjectProperty
comment: The next step(s) of the pathway. Contains zero or more pathwayStep instances. If there is no next step, this property is empty.
range: pathwayStep
domain: pathwayStep

ORGANISM
type: ObjectProperty
comment: An organism, e.g. 'Homo sapiens'. This is the organism that the entity is found in. Pathways may not have an organism associated with them, for instance, reference pathways from KEGG. Sequence-based entities (DNA, protein, RNA) may contain an xref to a sequence database that contains organism information, in which case the information should be consistent with the value for ORGANISM.
range: bioSource
domain: Class
  union of: complex
  union of: dna
  union of: pathway
  union of: protein
  union of: rna

PARTICIPANT
type: ObjectProperty
comment: The participant that has the experimental form being described.
domain: experimentalForm
range: physicalEntityParticipant

PARTICIPANTS
type: ObjectProperty
comment: This property lists the entities that participate in this interaction. For example, in a biochemical reaction, the participants are the union of the reactants and the products of the reaction. This property has a number of sub-properties, such as LEFT and RIGHT in the biochemicalInteraction class. Any participant listed in a sub-property will automatically be assumed to also be in PARTICIPANTS by a number of software systems, including Protégé, so this property should not contain any instances if there are instances contained in a sub-property.
domain: interaction
range: Class
  union of: entity
  union of: physicalEntityParticipant

PATHWAY-COMPONENTS
type: ObjectProperty
comment: The set of interactions and/or pathwaySteps in this pathway/network. Each instance of the pathwayStep class defines: 1) a set of interactions that together define a particular step in the pathway, for example a catalysis instance and the conversion that it catalyzes; 2) an order relationship to one or more other pathway steps (via the NEXT-STEP property). Note: This ordering is not necessarily temporal - the order described may simply represent connectivity between adjacent steps. Temporal ordering information should only be inferred from the direction of each interaction.
domain: pathway
range: Class
  union of: interaction
  union of: pathway
  union of: pathwayStep

PHYSICAL-ENTITY
type: ObjectProperty
comment: The physical entity annotated with stoichiometry and cellular location attributes from the physicalEntityParticipant instance.
range: physicalEntity
domain: physicalEntityParticipant

RIGHT
type: ObjectProperty
comment: The participants on the right side of the conversion interaction. Since conversion interactions may proceed in either the left-to-right or right-to-left direction, occupants of the RIGHT property may be either reactants or products. RIGHT is a sub-property of PARTICIPANTS.
sub property of: PARTICIPANTS
domain: conversion
range: physicalEntityParticipant

SEQUENCE-FEATURE-LIST
type: ObjectProperty
comment: Sequence features relevant for the interaction, for example binding domains or modification sites. Warning: this property may be moved into a state class in Level 3.
range: sequenceFeature
domain: sequenceParticipant

SEQUENCE-INTERVAL-BEGIN
type: ObjectProperty
comment: The begin position of a sequence interval.
domain: sequenceInterval
range: sequenceSite

SEQUENCE-INTERVAL-END
type: ObjectProperty
comment: The end position of a sequence interval.
domain: sequenceInterval
range: sequenceSite

STEP-INTERACTIONS
type: ObjectProperty
comment: The interactions that take place at this step of the pathway.
domain: pathwayStep
range: Class
  union of: interaction
  union of: pathway

STRUCTURE
type: ObjectProperty
comment: Defines the chemical structure and other information about this molecule, using an instance of class chemicalStructure.
range: chemicalStructure
domain: smallMolecule

TAXON-XREF
type: ObjectProperty
comment: An xref to an organism taxonomy database, preferably NCBI taxon. This should be an instance of unificationXref, unless the organism is not in an existing database.
domain: bioSource
range: unificationXref

TISSUE
type: ObjectProperty
comment: An external controlled vocabulary of tissue types.
domain: bioSource
range: openControlledVocabulary

XREF
type: ObjectProperty
comment: Values of this property define external cross-references from this entity to entities in external databases.
range: xref
domain: Class
  union of: confidence
  union of: dataSource
  union of: entity
  union of: evidence
  union of: openControlledVocabulary
  union of: sequenceFeature

AUTHORS
type: DatatypeProperty
comment: The authors of this publication, one per property value.
domain: publicationXref
range: string

AVAILABILITY
type: DatatypeProperty
comment: Describes the availability of this data (e.g. a copyright statement).
domain: entity
range: string

CHEMICAL-FORMULA
type: DatatypeProperty
comment: The chemical formula of the small molecule. Note: chemical formula can also be stored in the STRUCTURE property (in CML). In case of disagreement between the value of this property and that in the CML file, the CML value takes precedence.
domain: smallMolecule
range: string

COMMENT
type: DatatypeProperty
comment: Comment on the data in the container class. This property should be used instead of the OWL documentation elements (rdfs:comment) for instances because information in COMMENT is data to be exchanged, whereas the rdfs:comment field is used for metadata about the structure of the BioPAX ontology.
range: string
domain: Class
  union of: entity
  union of: utilityClass

CONFIDENCE-VALUE
type: DatatypeProperty
comment: The value of the confidence measure.
domain: confidence
range: string

CONTROL-TYPE
type: DatatypeProperty
comment: Defines the nature of the control relationship between the CONTROLLER and the CONTROLLED entities. The following terms are possible values: ACTIVATION: General activation. Compounds that activate the specified enzyme activity by an unknown mechanism. The mechanism is defined as unknown, because either the mechanism has yet to be elucidated in the experimental literature, or the paper(s) curated thus far do not define the mechanism, and a full literature search has yet to be performed. The following term can not be used in the catalysis class: INHIBITION: General inhibition. Compounds that inhibit the specified enzyme activity by an unknown mechanism. The mechanism is defined as unknown, because either the mechanism has yet to be elucidated in the experimental literature, or the paper(s) curated thus far do not define the mechanism, and a full literature search has yet to be performed. The following terms can only be used in the modulation class (these definitions from EcoCyc): INHIBITION-ALLOSTERIC Allosteric inhibitors decrease the specified enzyme activity by binding reversibly to the enzyme and inducing a conformational change that decreases the affinity of the enzyme to its substrates without affecting its VMAX. Allosteric inhibitors can be competitive or noncompetitive inhibitors, therefore, those inhibition categories can be used in conjunction with this category. INHIBITION-COMPETITIVE Competitive inhibitors are compounds that competitively inhibit the specified enzyme activity by binding reversibly to the enzyme and preventing the substrate from binding. Binding of the inhibitor and substrate are mutually exclusive because it is assumed that the inhibitor and substrate can both bind only to the free enzyme. A competitive inhibitor can either bind to the active site of the enzyme, directly excluding the substrate from binding there, or it can bind to another site on the enzyme, altering the conformation of the enzyme such that the substrate can not bind to th…
domain: control
range: Datatype
  one of: ACTIVATION
  one of: ACTIVATION-ALLOSTERIC
  one of: ACTIVATION-NONALLOSTERIC
  one of: INHIBITION
  one of: INHIBITION-ALLOSTERIC
  one of: INHIBITION-COMPETITIVE
  one of: INHIBITION-IRREVERSIBLE
  one of: INHIBITION-NONCOMPETITIVE
  one of: INHIBITION-OTHER
  one of: INHIBITION-UNCOMPETITIVE

DB
type: DatatypeProperty
comment: The name of the external database to which this xref refers.
domain: xref
range: string

DB-VERSION
type: DatatypeProperty
comment: The version of the external database in which this xref was last known to be valid. Resources may have recommendations for referencing dataset versions. For instance, the Gene Ontology recommends listing the date the GO terms were downloaded.
domain: xref
range: string

DELTA-G-PRIME-O
type: DatatypeProperty
comment: For biochemical reactions, this property refers to the standard transformed Gibbs energy change for a reaction written in terms of biochemical reactants (sums of species), delta-G'o. delta-G'o = -RT lnK' and delta-G'o = delta-H'o - T delta-S'o delta-G'o has units of kJ/mol. Like K', it is a function of temperature (T), ionic strength (I), pH, and pMg (pMg = -log10[Mg2+]). Therefore, these quantities must be specified, and values for DELTA-G for biochemical reactions are represented as 5-tuples of the form (delta-G'o T I pH pMg). (This definition from EcoCyc)
domain: deltaGprimeO
range: float

DELTA-H
type: DatatypeProperty
comment: For biochemical reactions, this property refers to the standard transformed enthalpy change for a reaction written in terms of biochemical reactants (sums of species), delta-H'o. delta-G'o = delta-H'o - T delta-S'o Units: kJ/mole (This definition from EcoCyc)
domain: biochemicalReaction
range: double

DELTA-S
type: DatatypeProperty
comment: For biochemical reactions, this property refers to the standard transformed entropy change for a reaction written in terms of biochemical reactants (sums of species), delta-S'o. delta-G'o = delta-H'o - T delta-S'o (This definition from EcoCyc)
domain: biochemicalReaction
range: double

DIRECTION
type: DatatypeProperty
comment: Specifies the reaction direction of the interaction catalyzed by this instance of the catalysis class. Possible values of this slot are: REVERSIBLE: Interaction occurs in both directions in physiological settings. PHYSIOL-LEFT-TO-RIGHT PHYSIOL-RIGHT-TO-LEFT The interaction occurs in the specified direction in physiological settings, because of several possible factors including the energetics of the reaction, local concentrations of reactants and products, and the regulation of the enzyme or its expression. IRREVERSIBLE-LEFT-TO-RIGHT IRREVERSIBLE-RIGHT-TO-LEFT For all practical purposes, the interactions occurs only in the specified direction in physiological settings, because of chemical properties of the reaction. (This definition from EcoCyc)
domain: catalysis
range: Datatype
  one of: IRREVERSIBLE-LEFT-TO-RIGHT
  one of: IRREVERSIBLE-RIGHT-TO-LEFT
  one of: PHYSIOL-LEFT-TO-RIGHT
  one of: PHYSIOL-RIGHT-TO-LEFT
  one of: REVERSIBLE

EC-NUMBER
type: DatatypeProperty
comment: The unique number assigned to a reaction by the Enzyme Commission of the International Union of Biochemistry and Molecular Biology. Note that not all biochemical reactions currently have EC numbers assigned to them.
domain: biochemicalReaction
range: string

ID
type: DatatypeProperty
comment: The primary identifier in the external database of the object to which this xref refers.
domain: xref
range: string

ID-VERSION
type: DatatypeProperty
comment: The version number of the identifier (ID). E.g. The RefSeq accession number NM_005228.3 should be split into NM_005228 as the ID and 3 as the ID-VERSION.
domain: xref
range: string

IONIC-STRENGTH
type: DatatypeProperty
comment: The ionic strength is defined as half of the total sum of the concentration (ci) of every ionic species (i) in the solution times the square of its charge (zi). For example, the ionic strength of a 0.1 M solution of CaCl2 is 0.5 x (0.1 x 22 + 0.2 x 12) = 0.3 M (Definition from http://www.lsbu.ac.uk/biology/enztech/ph.html)
range: float
domain: Class
  union of: deltaGprimeO
  union of: kPrime

K-PRIME
type: DatatypeProperty
comment: The apparent equilibrium constant K'. Concentrations in the equilibrium constant equation refer to the total concentrations of all forms of particular biochemical reactants. For example, in the equilibrium constant equation for the biochemical reaction in which ATP is hydrolyzed to ADP and inorganic phosphate: K' = [ADP][Pi]/[ATP], The concentration of ATP refers to the total concentration of all of the following species: [ATP] = [ATP4-] + [HATP3-] + [H2ATP2-] + [MgATP2-] + [MgHATP-] + [Mg2ATP]. The apparent equilibrium constant is formally dimensionless, and can be kept so by inclusion of as many of the terms (1 mol/dm3) in the numerator or denominator as necessary. It is a function of temperature (T), ionic strength (I), pH, and pMg (pMg = -log10[Mg2+]). (Definition from EcoCyc)
domain: kPrime
range: float

MOLECULAR-WEIGHT
type: DatatypeProperty
comment: Defines the molecular weight of the molecule, in daltons.
domain: smallMolecule
range: double

NAME
type: DatatypeProperty
comment: The preferred full name for this entity.
range: string
domain: Class
  union of: bioSource
  union of: dataSource
  union of: entity
  union of: sequenceFeature

PH
type: DatatypeProperty
comment: A measure of acidity and alkalinity of a solution that is a number on a scale on which a value of 7 represents neutrality and lower numbers indicate increasing acidity and higher numbers increasing alkalinity and on which each unit of change represents a tenfold change in acidity or alkalinity and that is the negative logarithm of the effective hydrogen-ion concentration or hydrogen-ion activity in gram equivalents per liter of the solution. (Definition from Merriam-Webster Dictionary)
range: float
domain: Class
  union of: deltaGprimeO
  union of: kPrime

PMG
type: DatatypeProperty
comment: A measure of the concentration of magnesium (Mg) in solution. (pMg = -log10[Mg2+])
range: float
domain: Class
  union of: deltaGprimeO
  union of: kPrime

POSITION-STATUS
type: DatatypeProperty
comment: The confidence status of the sequence position. This could be: EQUAL: The SEQUENCE-POSITION is known to be at the SEQUENCE-POSITION. GREATER-THAN: The site is greater than the SEQUENCE-POSITION. LESS-THAN: The site is less than the SEQUENCE-POSITION.
domain: sequenceSite
range: Datatype
  one of: EQUAL
  one of: GREATER-THAN
  one of: LESS-THAN

RELATIONSHIP-TYPE
type: DatatypeProperty
comment: This property names the type of relationship between the BioPAX object linked from, and the external object linked to, such as 'gene of this protein', or 'protein with similar sequence'.
domain: relationshipXref
range: string

SEQUENCE
type: DatatypeProperty
comment: Polymer sequence in uppercase letters. For DNA, usually A,C,G,T letters representing the nucleosides of adenine, cytosine, guanine and thymine, respectively; for RNA, usually A, C, U, G; for protein, usually the letters corresponding to the 20 letter IUPAC amino acid code.
range: string
domain: Class
  union of: dna
  union of: protein
  union of: rna

SEQUENCE-POSITION
type: DatatypeProperty
comment: The integer listed gives the position. The first base or amino acid is position 1. In combination with the numeric value, the property 'POSITION-STATUS' allows to express fuzzy positions, e.g. 'less than 4'.
domain: sequenceSite
range: integer

SHORT-NAME
type: DatatypeProperty
comment: An abbreviated name for this entity, preferably a name that is short enough to be used in a visualization application to label a graphical element that represents this entity. If no short name is available, an xref may be used for this purpose by the visualization application.
range: string
domain: Class
  union of: entity
  union of: sequenceFeature

SOURCE
type: DatatypeProperty
comment: The source in which the reference was published, such as: a book title, or a journal title and volume and pages.
domain: publicationXref
range: string

SPONTANEOUS
type: DatatypeProperty
comment: Specifies whether a conversion occurs spontaneously (i.e. uncatalyzed, under biological conditions) left-to-right, right-to-left, or not at all. If the spontaneity is not known, the SPONTANEOUS property should be left empty.
domain: conversion
range: Datatype
  one of: L-R
  one of: NOT-SPONTANEOUS
  one of: R-L

STOICHIOMETRIC-COEFFICIENT
type: DatatypeProperty
comment: Each value of this property represents the stoichiometric coefficient for one of the physical entities in an interaction or complex. For a given interaction, the stoichiometry should always be used where possible instead of representing the number of participants with separate instances of each participant. If there are three ATP molecules, one ATP molecule should be represented as a participant and the stoichiometry should be set to 3.
domain: physicalEntityParticipant
range: double

STRUCTURE-DATA
type: DatatypeProperty
comment: This property holds a string of data defining chemical structure or other information, in either the CML or SMILES format, as specified in property Structure-Format. If, for example, the CML format is used, then the value of this property is a string containing the XML encoding of the CML data.
domain: chemicalStructure
range: string

STRUCTURE-FORMAT
type: DatatypeProperty
comment: This property specifies which format is used to define chemical structure data.
domain: chemicalStructure
range: Datatype
  one of: CML
  one of: InChI
  one of: SMILES

SYNONYMS
type: DatatypeProperty
comment: One or more synonyms for the name of this entity. This should include the values of the NAME and SHORT-NAME property so that it is easy to find all known names in one place.
range: string
domain: Class
  union of: entity
  union of: sequenceFeature

TEMPERATURE
type: DatatypeProperty
comment: Temperature in Celsius
range: float
domain: Class
  union of: deltaGprimeO
  union of: kPrime

TERM
type: DatatypeProperty
comment: The external controlled vocabulary term.
domain: openControlledVocabulary
range: string

TITLE
type: DatatypeProperty
comment: The title of the publication.
domain: publicationXref
range: string

URL
type: DatatypeProperty
comment: The URL at which the publication can be found, if it is available through the Web.
domain: publicationXref
range: string

YEAR
type: DatatypeProperty
comment: The year in which this publication was published.
domain: publicationXref
range: int

bioSource
type: Class
subclass of: externalReferenceUtilityClass
subclass of: Restriction
  on property: TAXON-XREF
  cardinality: 1
subclass of: Restriction
  on property: NAME
  max cardinality: 1
subclass of: Restriction
  on property: TISSUE
  max cardinality: 1
subclass of: Restriction
  on property: CELLTYPE
  max cardinality: 1
disjoint with: dataSource
disjoint with: openControlledVocabulary
disjoint with: xref
comment: Definition: The biological source of an entity (e.g. protein, RNA or DNA). Some entities are considered source-neutral (e.g. small molecules), and the biological source of others can be deduced from their constituentss (e.g. complex, pathway). Examples: HeLa cells, human, and mouse liver tissue.

biochemicalReaction
type: Class
subclass of: conversion
disjoint with: complexAssembly
comment: Definition: A conversion interaction in which one or more entities (substrates) undergo covalent changes to become one or more other entities (products). The substrates of biochemical reactions are defined in terms of sums of species. This is convention in biochemistry, and, in principle, all of the EC reactions should be biochemical reactions. Examples: ATP + H2O = ADP + Pi Comment: In the example reaction above, ATP is considered to be an equilibrium mixture of several species, namely ATP4-, HATP3-, H2ATP2-, MgATP2-, MgHATP-, and Mg2ATP. Additional species may also need to be considered if other ions (e.g. Ca2+) that bind ATP are present. Similar considerations apply to ADP and to inorganic phosphate (Pi). When writing biochemical reactions, it is not necessary to attach charges to the biochemical reactants or to include ions such as H+ and Mg2+ in the equation. The reaction is written in the direction specified by the EC nomenclature system, if applicable, regardless of the physiological direction(s) in which the reaction proceeds. Polymerization reactions involving large polymers whose structure is not explicitly captured should generally be represented as unbalanced reactions in which the monomer is consumed but the polymer remains unchanged, e.g. glycogen + glucose = glycogen.

catalysis
type: Class
subclass of: control
subclass of: Restriction
  on property: CONTROLLED
  max cardinality: 1
subclass of: Restriction
  on property: CONTROLLER
  max cardinality: 1
subclass of: Restriction
  on property: CONTROL-TYPE
  has value: ACTIVATION
subclass of: Restriction
  on property: CONTROLLED
  all values from: conversion
subclass of: Restriction
  on property: DIRECTION
  max cardinality: 1
disjoint with: modulation
comment: Definition: A control interaction in which a physical entity (a catalyst) increases the rate of a conversion interaction by lowering its activation energy. Instances of this class describe a pairing between a catalyzing entity and a catalyzed conversion. Comment: A separate catalysis instance should be created for each different conversion that a physicalEntity may catalyze and for each different physicalEntity that may catalyze a conversion. For example, a bifunctional enzyme that catalyzes two different biochemical reactions would be linked to each of those biochemical reactions by two separate instances of the catalysis class. Also, catalysis reactions from multiple different organisms could be linked to the same generic biochemical reaction (a biochemical reaction is generic if it only includes small molecules). Generally, the enzyme catalyzing a conversion is known and the use of this class is obvious. In the cases where a catalyzed reaction is known to occur but the enzyme is not known, a catalysis instance should be created without a controller specified (i.e. the CONTROLLER property should remain empty). Synonyms: facilitation, acceleration. Examples: The catalysis of a biochemical reaction by an enzyme, the enabling of a transport interaction by a membrane pore complex, and the facilitation of a complex assembly by a scaffold protein. Hexokinase -> (The "Glucose + ATP -> Glucose-6-phosphate +ADP" reaction). A plasma membrane Na+/K+ ATPase is an active transporter (antiport pump) using the energy of ATP to pump Na+ out of the cell and K+ in. Na+ from cytoplasm to extracellular space would be described in a transport instance. K+ from extracellular space to cytoplasm would be described in a transport instance. The ATPase pump would be stored in a catalysis instance controlling each of the above transport instances. A biochemical reaction that does not occur by itself under physiological conditions, but has been observed to occur in the presence of cell extrac…

chemicalStructure
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: STRUCTURE-FORMAT
  cardinality: 1
subclass of: Restriction
  on property: STRUCTURE-DATA
  cardinality: 1
disjoint with: confidence
disjoint with: deltaGprimeO
disjoint with: evidence
disjoint with: experimentalForm
disjoint with: externalReferenceUtilityClass
disjoint with: kPrime
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: Describes a small molecule structure. Structure information is stored in the property STRUCTURE-DATA, in one of three formats: the CML format (see URL www.xml-cml.org), the SMILES format (see URL www.daylight.com/dayhtml/smiles/) or the InChI format (http://www.iupac.org/inchi/). The STRUCTURE-FORMAT property specifies which format is used. Comment: By virtue of the expressivity of CML, an instance of this class can also provide additional information about a small molecule, such as its chemical formula, names, and synonyms, if CML is used as the structure format. Examples: The following SMILES string, which describes the structure of glucose-6-phosphate: 'C(OP(=O)(O)O)[CH]1([CH](O)[CH](O)[CH](O)[CH](O)O1)'.

complex
type: Class
subclass of: physicalEntity
disjoint with: dna
disjoint with: protein
disjoint with: rna
disjoint with: smallMolecule
comment: Definition: A physical entity whose structure is comprised of other physical entities bound to each other non-covalently, at least one of which is a macromolecule (e.g. protein, DNA, or RNA). Complexes must be stable enough to function as a biological unit; in general, the temporary association of an enzyme with its substrate(s) should not be considered or represented as a complex. A complex is the physical product of an interaction (complexAssembly) and is not itself considered an interaction. Comment: In general, complexes should not be defined recursively so that smaller complexes exist within larger complexes, i.e. a complex should not be a COMPONENT of another complex (see comments on the COMPONENT property). The boundaries on the size of complexes described by this class are not defined here, although elements of the cell as large and dynamic as, e.g., a mitochondrion would typically not be described using this class (later versions of this ontology may include a cellularComponent class to represent these). The strength of binding and the topology of the components cannot be described currently, but may be included in future versions of the ontology, depending on community need. Examples: Ribosome, RNA polymerase II. Other examples of this class include complexes of multiple protein monomers and complexes of proteins and small molecules.

complexAssembly
type: Class
subclass of: conversion
disjoint with: transport
comment: Definition: A conversion interaction in which a set of physical entities, at least one being a macromolecule (e.g. protein, RNA, DNA), aggregate via non-covalent interactions. One of the participants of a complexAssembly must be an instance of the class complex (via a physicalEntityParticipant instance). Comment: This class is also used to represent complex disassembly. The assembly or disassembly of a complex is often a spontaneous process, in which case the direction of the complexAssembly (toward either assembly or disassembly) should be specified via the SPONTANEOUS property. Synonyms: aggregation, complex formation Examples: Assembly of the TFB2 and TFB3 proteins into the TFIIH complex, and assembly of the ribosome through aggregation of its subunits. Note: The following are not examples of complex assembly: Covalent phosphorylation of a protein (this is a biochemicalReaction); the TFIIH complex itself (this is an instance of the complex class, not the complexAssembly class).

confidence
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: CONFIDENCE-VALUE
  cardinality: 1
subclass of: Restriction
  on property: XREF
  min cardinality: 1
subclass of: Restriction
  on property: XREF
  all values from: publicationXref
disjoint with: deltaGprimeO
disjoint with: evidence
disjoint with: experimentalForm
disjoint with: externalReferenceUtilityClass
disjoint with: kPrime
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: Confidence that the containing instance actually occurs or exists in vivo, usually a statistical measure. The xref must contain at least on publication that describes the method used to determine the confidence. There is currently no standard way of describing confidence values, so any string is valid for the confidence value. In the future, a controlled vocabulary of accepted confidence values could become available, in which case it will likely be adopted for use here to describe the value. Examples: The statistical significance of a result, e.g. "p<0.05".

control
type: Class
subclass of: physicalInteraction
subclass of: Restriction
  on property: CONTROL-TYPE
  max cardinality: 1
disjoint with: conversion
comment: Definition: An interaction in which one entity regulates, modifies, or otherwise influences another. Two types of control interactions are defined: activation and inhibition. Comment: In general, the targets of control processes (i.e. occupants of the CONTROLLED property) should be interactions. Conceptually, physical entities are involved in interactions (or events) and the events should be controlled or modified, not the physical entities themselves. For example, a kinase activating a protein is a frequent event in signaling pathways and is usually represented as an 'activation' arrow from the kinase to the substrate in signaling diagrams. This is an abstraction that can be ambiguous out of context. In BioPAX, this information should be captured as the kinase catalyzing (via an instance of the catalysis class) a reaction in which the substrate is phosphorylated, instead of as a control interaction in which the kinase activates the substrate. Since this class is a superclass for specific types of control, instances of the control class should only be created when none of its subclasses are applicable. Synonyms: regulation, mediation Examples: A small molecule that inhibits a pathway by an unknown mechanism controls the pathway.

conversion
type: Class
subclass of: physicalInteraction
subclass of: Restriction
  on property: PARTICIPANTS
  all values from: physicalEntityParticipant
subclass of: Restriction
  on property: SPONTANEOUS
  max cardinality: 1
comment: Definition: An interaction in which one or more entities is physically transformed into one or more other entities. Comment: This class is designed to represent a simple, single-step transformation. Multi-step transformations, such as the conversion of glucose to pyruvate in the glycolysis pathway, should be represented as pathways, if known. Since it is a highly abstract class in the ontology, instances of the conversion class should never be created. Examples: A biochemical reaction converts substrates to products, the process of complex assembly converts single molecules to a complex, transport converts entities in one compartment to the same entities in another compartment.

dataSource
type: Class
subclass of: externalReferenceUtilityClass
subclass of: Restriction
  on property: XREF
  all values from: Class
    union of: publicationXref
    union of: unificationXref
disjoint with: openControlledVocabulary
disjoint with: xref
comment: Definition: The direct source of this data. This does not store the trail of sources from the generation of the data to this point, only the last known source, such as a database. The XREF property may contain a publicationXref referencing a publication describing the data source (e.g. a database publication). A unificationXref may be used e.g. when pointing to an entry in a database of databases describing this database. Examples: A database or person name.

deltaGprimeO
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: PH
  max cardinality: 1
subclass of: Restriction
  on property: IONIC-STRENGTH
  max cardinality: 1
subclass of: Restriction
  on property: TEMPERATURE
  max cardinality: 1
subclass of: Restriction
  on property: DELTA-G-PRIME-O
  cardinality: 1
subclass of: Restriction
  on property: PMG
  max cardinality: 1
disjoint with: evidence
disjoint with: experimentalForm
disjoint with: externalReferenceUtilityClass
disjoint with: kPrime
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: For biochemical reactions, this property refers to the standard transformed Gibbs energy change for a reaction written in terms of biochemical reactants (sums of species), delta-G'o. delta-G'o = -RT lnK' and delta-G'o = delta-H'o - T delta-S'o delta-G'o has units of kJ/mol. Like K', it is a function of temperature (T), ionic strength (I), pH, and pMg (pMg = -log10[Mg2+]). Therefore, these quantities must be specified, and values for DELTA-G for biochemical reactions are represented as 5-tuples of the form (delta-G'o T I pH pMg). This property may have multiple values, representing different measurements for delta-G'o obtained under the different experimental conditions listed in the 5-tuple. (This definition from EcoCyc)

dna
type: Class
subclass of: physicalEntity
disjoint with: protein
disjoint with: rna
disjoint with: smallMolecule
comment: Definition: A physical entity consisting of a sequence of deoxyribonucleotide monophosphates; a deoxyribonucleic acid. Comment: This is not a 'gene', since gene is a genetic concept, not a physical entity. The concept of a gene may be added later in BioPAX. Examples: a chromosome, a plasmid. A specific example is chromosome 7 of Homo sapiens.

entity
type: Class
subclass of: Thing
subclass of: Restriction
  on property: NAME
  max cardinality: 1
subclass of: Restriction
  on property: SHORT-NAME
  max cardinality: 1
disjoint with: utilityClass
comment: Definition: A discrete biological unit used when describing pathways. Comment: This is the root class for all biological concepts in the ontology, which include pathways, interactions and physical entities. As the most abstract class in the ontology, instances of the entity class should never be created. Instead, more specific classes should be used. Synonyms: thing, object, bioentity.

evidence
type: Class
subclass of: utilityClass
subclass of: Class
  union of: Restriction
    on property: CONFIDENCE
    min cardinality: 1
  union of: Restriction
    on property: EVIDENCE-CODE
    min cardinality: 1
  union of: Restriction
    on property: EXPERIMENTAL-FORM
    min cardinality: 1
disjoint with: experimentalForm
disjoint with: externalReferenceUtilityClass
disjoint with: kPrime
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: The support for a particular assertion, such as the existence of an interaction or pathway. At least one of CONFIDENCE, EVIDENCE-CODE, or EXPERIMENTAL-FORM must be instantiated when creating an evidence instance. XREF may reference a publication describing the experimental evidence using a publicationXref or may store a description of the experiment in an experimental description database using a unificationXref (if the referenced experiment is the same) or relationshipXref (if it is not identical, but similar in some way e.g. similar in protocol). Evidence is meant to provide more information than just an xref to the source paper. Examples: A description of a molecular binding assay that was used to detect a protein-protein interaction.

experimentalForm
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: PARTICIPANT
  cardinality: 1
subclass of: Restriction
  on property: EXPERIMENTAL-FORM-TYPE
  min cardinality: 1
disjoint with: externalReferenceUtilityClass
disjoint with: kPrime
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: The form of a physical entity in a particular experiment, as it may be modified for purposes of experimental design. Examples: A His-tagged protein in a binding assay. A protein can be tagged by multiple tags, so can have more than 1 experimental form type terms

externalReferenceUtilityClass
type: Class
subclass of: utilityClass
disjoint with: kPrime
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: A pointer to an external object, such as an entry in a database or a term in a controlled vocabulary. Comment: This class is for organizational purposes only; direct instances of this class should not be created.

interaction
type: Class
subclass of: entity
subclass of: Restriction
  on property: PARTICIPANTS
  some values from: Class
    union of: entity
    union of: physicalEntityParticipant
disjoint with: pathway
disjoint with: physicalEntity
comment: Definition: A single biological relationship between two or more entities. An interaction cannot be defined without the entities it relates. Comment: Since it is a highly abstract class in the ontology, instances of the interaction class should never be created. Instead, more specific classes should be used. Currently this class only has subclasses that define physical interactions; later levels of BioPAX may define other types of interactions, such as genetic (e.g. synthetic lethal). Naming rationale: A number of names were considered for this concept, including "process", "synthesis" and "relationship"; Interaction was chosen as it is understood by biologists in a biological context and is compatible with PSI-MI. Examples: protein-protein interaction, biochemical reaction, enzyme catalysis

kPrime
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: PH
  max cardinality: 1
subclass of: Restriction
  on property: K-PRIME
  cardinality: 1
subclass of: Restriction
  on property: IONIC-STRENGTH
  max cardinality: 1
subclass of: Restriction
  on property: PMG
  max cardinality: 1
subclass of: Restriction
  on property: TEMPERATURE
  max cardinality: 1
disjoint with: pathwayStep
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: The apparent equilibrium constant, K', and associated values. Concentrations in the equilibrium constant equation refer to the total concentrations of all forms of particular biochemical reactants. For example, in the equilibrium constant equation for the biochemical reaction in which ATP is hydrolyzed to ADP and inorganic phosphate: K' = [ADP][Pi]/[ATP], The concentration of ATP refers to the total concentration of all of the following species: [ATP] = [ATP4-] + [HATP3-] + [H2ATP2-] + [MgATP2-] + [MgHATP-] + [Mg2ATP]. The apparent equilibrium constant is formally dimensionless, and can be kept so by inclusion of as many of the terms (1 mol/dm3) in the numerator or denominator as necessary. It is a function of temperature (T), ionic strength (I), pH, and pMg (pMg = -log10[Mg2+]). Therefore, these quantities must be specified to be precise, and values for KEQ for biochemical reactions may be represented as 5-tuples of the form (K' T I pH pMg). This property may have multiple values, representing different measurements for K' obtained under the different experimental conditions listed in the 5-tuple. (This definition adapted from EcoCyc) See http://www.chem.qmul.ac.uk/iubmb/thermod/ for a thermodynamics tutorial.

modulation
type: Class
subclass of: control
subclass of: Restriction
  on property: CONTROLLED
  max cardinality: 1
subclass of: Restriction
  on property: CONTROLLER
  max cardinality: 1
subclass of: Restriction
  on property: CONTROLLED
  all values from: catalysis
comment: Definition: A control interaction in which a physical entity modulates a catalysis interaction. Biologically, most modulation interactions describe an interaction in which a small molecule alters the ability of an enzyme to catalyze a specific reaction. Instances of this class describe a pairing between a modulating entity and a catalysis interaction. Comment: A separate modulation instance should be created for each different catalysis instance that a physical entity may modulate and for each different physical entity that may modulate a catalysis instance. A typical modulation instance has a small molecule as the controller entity and a catalysis instance as the controlled entity. Examples: Allosteric activation and competitive inhibition of an enzyme's ability to catalyze a specific reaction.

openControlledVocabulary
type: Class
subclass of: externalReferenceUtilityClass
subclass of: Restriction
  on property: XREF
  all values from: unificationXref
disjoint with: xref
comment: Definition: Used to import terms from external controlled vocabularies (CVs) into the ontology. To support consistency and compatibility, open, freely available CVs should be used whenever possible, such as the Gene Ontology (GO) or other open biological CVs listed on the OBO website (http://obo.sourceforge.net/). Comment: The ID property in unification xrefs to GO and other OBO ontologies should include the ontology name in the ID property (e.g. ID="GO:0005634" instead of ID="0005634").

pathway
type: Class
subclass of: entity
subclass of: Restriction
  on property: ORGANISM
  max cardinality: 1
disjoint with: physicalEntity
comment: Definition: A set or series of interactions, often forming a network, which biologists have found useful to group together for organizational, historic, biophysical or other reasons. Comment: It is possible to define a pathway without specifying the interactions within the pathway. In this case, the pathway instance could consist simply of a name and could be treated as a 'black box'. Synonyms: network Examples: glycolysis, valine biosynthesis

pathwayStep
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: STEP-INTERACTIONS
  min cardinality: 1
disjoint with: physicalEntityParticipant
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: A step in a pathway. Comment: Multiple interactions may occur in a pathway step, each should be listed in the STEP-INTERACTIONS property. Order relationships between pathway steps may be established with the NEXT-STEP slot. This order may not be temporally meaningful for specific steps, such as for a pathway loop or a reversible reaction, but represents a directed graph of step relationships that can be useful for describing the overall flow of a pathway, as may be useful in a pathway diagram. Example: A metabolic pathway may contain a pathway step composed of one biochemical reaction (BR1) and one catalysis (CAT1) instance, where CAT1 describes the catalysis of BR1.

physicalEntity
type: Class
subclass of: entity
comment: Definition: An entity with a physical structure. A pool of entities, not a specific molecular instance of an entity in a cell. Comment: This class serves as the super-class for all physical entities, although its current set of subclasses is limited to molecules. As a highly abstract class in the ontology, instances of the physicalEntity class should never be created. Instead, more specific classes should be used. Synonyms: part, interactor, object Naming rationale: It's difficult to find a name that encompasses all of the subclasses of this class without being too general. E.g. PSI-MI uses 'interactor', BIND uses 'object', BioCyc uses 'chemicals'. physicalEntity seems to be a good name for this specialization of entity. Examples: protein, small molecule, RNA

physicalEntityParticipant
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: PHYSICAL-ENTITY
  cardinality: 1
subclass of: Restriction
  on property: CELLULAR-LOCATION
  max cardinality: 1
subclass of: Restriction
  on property: STOICHIOMETRIC-COEFFICIENT
  max cardinality: 1
disjoint with: sequenceFeature
disjoint with: sequenceLocation
comment: Definition: Any additional special characteristics of a physical entity in the context of an interaction or complex. These currently include stoichiometric coefficient and cellular location, but this list may be expanded in later levels. Comment: PhysicalEntityParticipants should not be used in multiple interaction or complex instances. Instead, each interaction and complex should reference its own unique set of physicalEntityParticipants. The reason for this is that a user may add new information about a physicalEntityParticipant for one interaction or complex, such as the presence of a previously unknown post-translational modification, and unwittingly invalidate the physicalEntityParticipant for the other interactions or complexes that make use of it. Example: In the interaction describing the transport of L-arginine into the cytoplasm in E. coli, the LEFT property in the interaction would be filled with an instance of physicalEntityParticipant that specified the location of L-arginine as periplasm and the stoichiometric coefficient as one.

physicalInteraction
type: Class
subclass of: interaction
subclass of: Restriction
  on property: PARTICIPANTS
  some values from: physicalEntityParticipant
comment: Definition: An interaction in which at least one participant is a physical entity, e.g. a binding event. Comment: This class should be used by default for representing molecular interactions, such as those defined by PSI-MI level 2. The participants in a molecular interaction should be listed in the PARTICIPANTS slot. Note that this is one of the few cases in which the PARTICPANT slot should be directly populated with instances (see comments on the PARTICPANTS property in the interaction class description). If sufficient information on the nature of a molecular interaction is available, a more specific BioPAX interaction class should be used. Example: Two proteins observed to interact in a yeast-two-hybrid experiment where there is not enough experimental evidence to suggest that the proteins are forming a complex by themselves without any indirect involvement of other proteins. This is the case for most large-scale yeast two-hybrid screens.

protein
type: Class
subclass of: physicalEntity
subclass of: Restriction
  on property: SEQUENCE
  max cardinality: 1
subclass of: Restriction
  on property: ORGANISM
  max cardinality: 1
disjoint with: rna
disjoint with: smallMolecule
comment: Definition: A physical entity consisting of a sequence of amino acids; a protein monomer; a single polypeptide chain. Examples: The epidermal growth factor receptor (EGFR) protein.

publicationXref
type: Class
subclass of: xref
subclass of: Restriction
  on property: TITLE
  max cardinality: 1
subclass of: Restriction
  on property: YEAR
  max cardinality: 1
disjoint with: relationshipXref
disjoint with: unificationXref
comment: Definition: An xref that defines a reference to a publication such as a book, journal article, web page, or software manual. The reference may or may not be in a database, although references to PubMed are preferred when possible. The publication should make a direct reference to the instance it is attached to. Comment: Publication xrefs should make use of PubMed IDs wherever possible. The DB property of an xref to an entry in PubMed should use the string "PubMed" and not "MEDLINE". Examples: PubMed:10234245

relationshipXref
type: Class
subclass of: xref
subclass of: Restriction
  on property: ID
  cardinality: 1
subclass of: Restriction
  on property: RELATIONSHIP-TYPE
  cardinality: 1
subclass of: Restriction
  on property: DB
  cardinality: 1
disjoint with: unificationXref
comment: Definition: An xref that defines a reference to an entity in an external resource that does not have the same biological identity as the referring entity. Comment: There is currently no controlled vocabulary of relationship types for BioPAX, although one will be created in the future if a need develops. Examples: A link between a gene G in a BioPAX data collection, and the protein product P of that gene in an external database. This is not a unification xref because G and P are different biological entities (one is a gene and one is a protein). Another example is a relationship xref for a protein that refers to the Gene Ontology biological process, e.g. 'immune response,' that the protein is involved in.

rna
type: Class
subclass of: physicalEntity
subclass of: Restriction
  on property: SEQUENCE
  max cardinality: 1
subclass of: Restriction
  on property: ORGANISM
  max cardinality: 1
disjoint with: smallMolecule
comment: Definition: A physical entity consisting of a sequence of ribonucleotide monophosphates; a ribonucleic acid. Examples: messengerRNA, microRNA, ribosomalRNA. A specific example is the let-7 microRNA.

sequenceFeature
type: Class
subclass of: utilityClass
subclass of: Restriction
  on property: SHORT-NAME
  max cardinality: 1
subclass of: Restriction
  on property: NAME
  max cardinality: 1
subclass of: Restriction
  on property: FEATURE-TYPE
  cardinality: 1
disjoint with: sequenceInterval
disjoint with: sequenceLocation
disjoint with: sequenceSite
comment: Definition: A feature on a sequence relevant to an interaction, such as a binding site or post-translational modification. Examples: A phosphorylation on a protein.

sequenceInterval
type: Class
subclass of: sequenceLocation
subclass of: Restriction
  on property: SEQUENCE-INTERVAL-END
  cardinality: 1
subclass of: Restriction
  on property: SEQUENCE-INTERVAL-BEGIN
  cardinality: 1
disjoint with: sequenceSite
comment: Definition: Describes an interval on a sequence. All of the sequence from the begin site to the end site (inclusive) is described, not any subset.

sequenceLocation
type: Class
subclass of: utilityClass
comment: Definition: A location on a nucleotide or amino acid sequence. Comment: For organizational purposes only; direct instances of this class should not be created.

sequenceParticipant
type: Class
subclass of: physicalEntityParticipant
comment: Definition: A DNA, RNA or protein participant in an interaction. Comment: See physicalEntityParticipant for more documentation.

sequenceSite
type: Class
subclass of: sequenceLocation
subclass of: Restriction
  on property: SEQUENCE-POSITION
  cardinality: 1
subclass of: Restriction
  on property: POSITION-STATUS
  cardinality: 1
comment: Definition: Describes a site on a sequence, i.e. the position of a single nucleotide or amino acid.

smallMolecule
type: Class
subclass of: physicalEntity
subclass of: Restriction
  on property: MOLECULAR-WEIGHT
  max cardinality: 1
subclass of: Restriction
  on property: CHEMICAL-FORMULA
  max cardinality: 1
comment: Definition: Any bioactive molecule that is not a peptide, DNA, or RNA. Generally these are non-polymeric, but complex carbohydrates are not explicitly modeled as classes in this version of the ontology, thus are forced into this class. Comment: Recently, a number of small molecule databases have become available to cross-reference from this class. Examples: glucose, penicillin, phosphatidylinositol

transport
type: Class
subclass of: conversion
comment: Definition: A conversion interaction in which an entity (or set of entities) changes location within or with respect to the cell. A transport interaction does not include the transporter entity, even if one is required in order for the transport to occur. Instead, transporters are linked to transport interactions via the catalysis class. Comment: Transport interactions do not involve chemical changes of the participant(s). These cases are handled by the transportWithBiochemicalReaction class. Synonyms: translocation. Examples: The movement of Na+ into the cell through an open voltage-gated channel.

transportWithBiochemicalReaction
type: Class
subclass of: biochemicalReaction
subclass of: transport
comment: Definition: A conversion interaction that is both a biochemicalReaction and a transport. In transportWithBiochemicalReaction interactions, one or more of the substrates change both their location and their physical structure. Active transport reactions that use ATP as an energy source fall under this category, even if the only covalent change is the hydrolysis of ATP to ADP. Comment: This class was added to support a large number of transport events in pathway databases that have a biochemical reaction during the transport process. It is not expected that other double inheritance subclasses will be added to the ontology at the same level as this class. Examples: In the PEP-dependent phosphotransferase system, transportation of sugar into an E. coli cell is accompanied by the sugar's phosphorylation as it crosses the plasma membrane.

unificationXref
type: Class
subclass of: xref
subclass of: Restriction
  on property: ID
  cardinality: 1
subclass of: Restriction
  on property: DB
  cardinality: 1
comment: Definition: A unification xref defines a reference to an entity in an external resource that has the same biological identity as the referring entity. For example, if one wished to link from a database record, C, describing a chemical compound in a BioPAX data collection to a record, C', describing the same chemical compound in an external database, one would use a unification xref since records C and C' describe the same biological identity. Generally, unification xrefs should be used whenever possible, although there are cases where they might not be useful, such as application to application data exchange. Comment: Unification xrefs in physical entities are essential for data integration, but are less important in interactions. This is because unification xrefs on the physical entities in an interaction can be used to compute the equivalence of two interactions of the same type. An xref in a protein pointing to a gene, e.g. in the LocusLink database17, would not be a unification xref since the two entities do not have the same biological identity (one is a protein, the other is a gene). Instead, this link should be a captured as a relationship xref. References to an external controlled vocabulary term within the OpenControlledVocabulary class should use a unification xref where possible (e.g. GO:0005737). Examples: An xref in a protein instance pointing to an entry in the Swiss-Prot database, and an xref in an RNA instance pointing to the corresponding RNA sequence in the RefSeq database..

utilityClass
type: Class
comment: Definition: Utility classes are created when simple slots are insufficient to describe an aspect of an entity or to increase compatibility of this ontology with other standards. The utilityClass class is actually a metaclass and is only present to organize the other helper classes under one class hierarchy; instances of utilityClass should never be created.

xref
type: Class
subclass of: externalReferenceUtilityClass
subclass of: Restriction
  on property: ID
  max cardinality: 1
subclass of: Restriction
  on property: DB-VERSION
  max cardinality: 1
subclass of: Restriction
  on property: DB
  max cardinality: 1
subclass of: Restriction
  on property: ID-VERSION
  max cardinality: 1
comment: Definition: A reference from an instance of a class in this ontology to an object in an external resource. Comment: Instances of the xref class should never be created and more specific classes should be used instead.

bioSource43
type: NamedIndividual
type: bioSource
NAME: Escherichia coli K-12
TAXON-XREF: unificationXref44

biochemicalReaction113
type: NamedIndividual
type: biochemicalReaction
EC-NUMBER: 2.7.1.40
NAME: phosphoenolpyruvate dephosphorylation
SYNONYMS: pyruvate phosphorylation
LEFT: physicalEntityParticipant114
RIGHT: physicalEntityParticipant16
RIGHT: physicalEntityParticipant26
LEFT: physicalEntityParticipant33
RIGHT: physicalEntityParticipant85

biochemicalReaction13
type: NamedIndividual
type: biochemicalReaction
DELTA-G: -3.4
EC-NUMBER: 2.7.1.11
NAME: 6PFRUCTPHOS-RXN
COMMENT: This is a key control step in glycolysis |CITS: [79100775]|
SYNONYMS: fructose-6-phosphate phosphorylation
RIGHT: physicalEntityParticipant16
LEFT: physicalEntityParticipant22
RIGHT: physicalEntityParticipant26
RIGHT: physicalEntityParticipant29
LEFT: physicalEntityParticipant33
XREF: publicationXref14
XREF: publicationXref15

biochemicalReaction172
type: NamedIndividual
type: biochemicalReaction
EC-NUMBER: 1.2.1.12
DELTA-G: 1.5
SYNONYMS: GAPDH
SYNONYMS: TRIOSEPHOSPHATE DEHYDROGENASE
NAME: glyceraldehyde 3-phosphate oxidation
LEFT: physicalEntityParticipant173
RIGHT: physicalEntityParticipant177
LEFT: physicalEntityParticipant180
LEFT: physicalEntityParticipant184
RIGHT: physicalEntityParticipant188
XREF: publicationXref14

biochemicalReaction205
type: NamedIndividual
type: biochemicalReaction
EC-NUMBER: 2.7.2.3
COMMENT: In this reaction a phosphoryl group is transferred from the acyl phosphate of 1,3 diphosphoglycerate to ADP thereby forming ATP and 3-phosphoglycerate.|CITS:[90336971]|
NAME: phosphoglycerate phosphorylation
RIGHT: physicalEntityParticipant16
RIGHT: physicalEntityParticipant188
LEFT: physicalEntityParticipant33
LEFT: physicalEntityParticipant57

biochemicalReaction260
type: NamedIndividual
type: biochemicalReaction
DELTA-G: 0.4
EC-NUMBER: 5.3.1.9
SYNONYMS: HEXOSEPHOSPHATE ISOMERASE
SYNONYMS: OXOISOMERASE
NAME: PGLUCISOM-RXN
SYNONYMS: PHOSPHOGLUCOISOMERASE
SYNONYMS: PHOSPHOGLUCOSE ISOMERASE
SYNONYMS: PHOSPHOHEXOISOMERASE
SYNONYMS: PHOSPHOHEXOMUTASE
SYNONYMS: PHOSPHOHEXOSE ISOMERASE
SYNONYMS: PHOSPHOSACCHAROMUTASE
RIGHT: physicalEntityParticipant22
LEFT: physicalEntityParticipant261

biochemicalReaction295
type: NamedIndividual
type: biochemicalReaction
EC-NUMBER: 4.1.2.13
DELTA-G: 5.7
SYNONYMS: ALDOLASE
COMMENT: Dihydroxyacetone phosphate is also called glycerone phosphate. Of the total aldolase activity in cell-free extracts of E.coli grown on pyruvate and lactate, approx. 60 % was accounted for by aldolase 1. On the other hand, E.coli grown on glucose showed no aldolase 1 activity but had an increased aldolase 2 activity. |CITS: [73229139]| During growth with CO2 as a carbon source, only class I aldolase is produced but when acetate replaces CO2 the class II aldolase is made. Similarly, in E.coli the putative class I aldolase is only synthesized during growth on C3 compounds and not on glucose, implying that a class I aldolase is preferred for gluconeogenesis |CITS:[73229139]|
NAME: F16ALDOLASE-RXN
SYNONYMS: FRUCTOSE-1,6-BISPHOSPHATE TRIOSEPHOSPHATE-LYASE
RIGHT: physicalEntityParticipant180
RIGHT: physicalEntityParticipant228
LEFT: physicalEntityParticipant29

biochemicalReaction297
type: NamedIndividual
type: biochemicalReaction
EC-NUMBER: 5.3.1.1
SYNONYMS: PHOSPHOTRIOSE ISOMERASE
SYNONYMS: TRIOSEPHOSPHATE MUTASE
NAME: triose phosphate isomerization
LEFT: physicalEntityParticipant180
RIGHT: physicalEntityParticipant228

biochemicalReaction56
type: NamedIndividual
type: biochemicalReaction
DELTA-G: 1.1
NAME: 3PGAREARR-RXN
EC-NUMBER: 5.4.2.1
SYNONYMS: PGAM
SYNONYMS: PHOSPHOGLYCERATE PHOSPHOMUTASE
SYNONYMS: PHOSPHOGLYCEROMUTASE
LEFT: physicalEntityParticipant57
RIGHT: physicalEntityParticipant61

biochemicalReaction84
type: NamedIndividual
type: biochemicalReaction
DELTA-G: 0.4
SYNONYMS: 2-PHOSPHOGLYCERATE DEHYDRATASE
NAME: 2-phosphoglycerate dehydration
EC-NUMBER: 4.2.1.11
SYNONYMS: ENOLASE
LEFT: physicalEntityParticipant61
RIGHT: physicalEntityParticipant85
RIGHT: physicalEntityParticipant90

catalysis109
type: NamedIndividual
type: catalysis
COMMENT: Pyruvate kinase I is strongly activated by fructose 1,6 bisphosphate and shows sigmoid kinetics with respect to the substrate phophoenolpyruvate. The dependences of the reaction rate on the concentrations of phosphoenolpyruvate, Mg+2, and Mn+2 are sigmoid. These dependences become hyperbolic on addition of fructose 1,6 bisphosphate. The dependences of the reaction rate on the concentration of ADP are always hyperbolic. The catalytic active complex of E. coli pyruvate kinase is formed by only one conformational state of the enzyme, state R1. This state binds randomly the Mg+2 free ligands ADP or phosphoenolpyruvate. Thereafter, the active enzyme complex is formed by binding Mg+2-PEP or Mg+2ADP respectively. State R2 of coli pyruvate kinase binds randomly ADP and Mg+2. It is the only state in which Mg+2 can bind to the free enzyme. Mg+2 is not necesary for the binding of ADP, PEP an ATP. Mg+2 can inhibit either by binding to the state R2 or by lowering the concentration of Mg+2, free ADP and PEP through complex formation. ATP inhibits by virtue of three effects: increase in ionic strength, complex-formation with Mg+2 when this metal ion acts as an activator and binding to the state R3. However when conditions are such that Mg+2 is an inhibitor, then ATP is expected to activate because of complex formation with Mg+2. In general, one can say that the ligands Mg+2 and ATP cannot be classified as inhibitors or activators because their regulatory effect on the reaction rate depends on the concentration of the other ligands.|CITS:[81159972]| By addition of fructose-1,6-bisphosphate the sigmoid kinetics with respect to phosphoenolpyruvate and Mg+2 is abolished and the activity of the enzyme is described by classical saturation kinetics. This is explained by exclusive binding of fructose 1,6 bisphosphate at an allosteric site of the conformational state that forms the active complex. Ca+2 is an activator of the enzyme at low Mg+2 and Ca+2 concentrations; otherwise it is an in…
DIRECTION: REVERSIBLE
SYNONYMS: phosphoenol transphosphorylase
SYNONYMS: phosphoenolpyruvate kinase
SYNONYMS: pyruvate 2-0-phosphotransferase
SYNONYMS: pyruvate kinase
SYNONYMS: pyruvate kinase F
NAME: pyruvate kinase I
SYNONYMS: type I pyruvate kinase
CONTROLLED: biochemicalReaction113
COFACTOR: physicalEntityParticipant110
CONTROLLER: physicalEntityParticipant120
COFACTOR: physicalEntityParticipant5
COFACTOR: physicalEntityParticipant71

catalysis137
type: NamedIndividual
type: catalysis
COMMENT: Pyruvate kinase II displays only limited cooperativity amoung phosphoenolpyruvate binding sites and is allosterically activated by AMP and several sugar phosphates |CITS:[91315755]| The enzyme requires both bivalent and monovalent cations. |CITS: [90336973]|
DIRECTION: REVERSIBLE
SYNONYMS: pyruvate kinase A
NAME: pyruvate kinase II
SYNONYMS: type II pyruvate kinase
CONTROLLED: biochemicalReaction113
COFACTOR: physicalEntityParticipant110
CONTROLLER: physicalEntityParticipant138
COFACTOR: physicalEntityParticipant5
COFACTOR: physicalEntityParticipant71

catalysis161
type: NamedIndividual
type: catalysis
SYNONYMS: BPG-dependent PGAM2
SYNONYMS: D-phosphoglycerate 2,3-phosphomutase 2
COMMENT: E. coli contains three phosphoglycerate mutases. Two are 2,3-bisphosphoglyerate-dependent enzymes, encoded by the gpmA and gpmB genes. The third is a 2,3-bisphosphoglyerate-independent enzyme encoded by the pgmI gene. |CITS: [99364512]|
SYNONYMS: PGAM2
DIRECTION: REVERSIBLE
NAME: phosphoglycerate mutase 2
SYNONYMS: phosphoglycerate phosphomutase 2
SYNONYMS: phosphoglyceromutase 2
CONTROLLED: biochemicalReaction56
CONTROLLER: physicalEntityParticipant162

catalysis189
type: NamedIndividual
type: catalysis
SYNONYMS: GAPDH-A
DIRECTION: REVERSIBLE
COMMENT: The E.coli sequence contains a certain number of amino acids which are conserved in all GAPDHs so far sequenced and which are postulated to be directly implicated in the NAD+ binding or in the catalysis mechanism. |CITS:[85257641]| There appear to be only two active sites per molecule.|CITS:[79255500]| NAD required for the phosphorylation as well as the oxidation |CITS:[79255500]|
NAME: glyceraldehyde 3-phosphate dehydrogenase-A complex
SYNONYMS: triosephosphate dehydrogenase
CONTROLLED: biochemicalReaction172
CONTROLLER: physicalEntityParticipant190
XREF: publicationXref170
XREF: publicationXref203

catalysis2
type: NamedIndividual
type: catalysis
NAME: 6-phosphofructokinase-1
COMMENT: 90% of the activity present in the wild type strain is pfk-1. |CITS: [83294514]| The enzyme shows cooperative kinetics with the substrate fructose-6-phosphate but not with the other substrate ATP. |CITS: [85203917]| The reverse reaction does not participate in gluconeogenesis: fdp phosphatase mutants are deficient in gluconeogenesis.|CITS: [78194149]| Studies on phosphfructokinase-1 include subunit structure |CITS:[91255189]|, ligand binding |CITS: [91355204]| and pH dependence |CITS: [91255189]|. The allosteric properties of phosphofructokinase-1 are due in part to ligand binding and in part to the kinetics of the reaction. |CITS: [92144584]|
SYNONYMS: PFK I
DIRECTION: REVERSIBLE
SYNONYMS: fructose-6-p-1-kinase
SYNONYMS: fructose-6-phosphate-1-phosphotransferase
CONTROLLED: biochemicalReaction13
CONTROLLER: physicalEntityParticipant37
COFACTOR: physicalEntityParticipant5
XREF: publicationXref10
XREF: publicationXref11
XREF: publicationXref12
XREF: publicationXref3
XREF: publicationXref4
XREF: publicationXref8
XREF: publicationXref9

catalysis207
type: NamedIndividual
type: catalysis
SYNONYMS: 2,3-diphospho-D-glycerate
SYNONYMS: 2-phospho-D-glycerate phosphotransferase
SYNONYMS: 3-phosphoglycerate kinase
SYNONYMS: Glycerate 3-P kinase
DIRECTION: REVERSIBLE
COMMENT: The structure of Pgk determined crystallographically is best described as an open bi-lobal molecule. The active site of the enzyme lies deep in the cleft formed between the two lobes.|CITS:[90336971]| When purified enzymes were employed there was absolute dependence upon the respective substrates of the glycolytic pathway. There was no activity unless ATP and glycerate-3-P were both included.|CITS:[71230170]|
NAME: phosphoglycerate kinase
CONTROLLED: biochemicalReaction205
CONTROLLER: physicalEntityParticipant208

catalysis238
type: NamedIndividual
type: catalysis
NAME: 6-phosphofructokinase-2
SYNONYMS: PFK II
COMMENT: Pfk-2 is somewhat sensitive to inhibition by fructose-1,6-diphosphate and ATP. Pfk-2,unlike pfk-1, does not show cooperative interaction with fructose-6-phosphate, inhibition by PEP or activation by ADP. |CITS:[84262485]| MgATP is an inhibitor of pfk-2 and it provokes the tetramerization of the dimeric native enzyme.|CITS: [85289307],[88292964]| Its normal function is not known and in strains with pfk-1, pfkB may be deleted without apparent effect. |CITS: [83294514]| However in the absence of pfk-1, slow growth on sugars depends on pfk-2. Its loss causes complete inability to grow. |CITS: [84262485]| The distribution of the two phosphofructokinases is variable among enterobacteria and also among E.coli strains |CITS: [82027179]|
DIRECTION: REVERSIBLE
SYNONYMS: fructose-6-p-1-kinase
SYNONYMS: fructose-6-phosphate-1-phosphotransferase
CONTROLLED: biochemicalReaction13
CONTROLLER: physicalEntityParticipant240
XREF: publicationXref239
XREF: publicationXref244

catalysis293
type: NamedIndividual
type: catalysis
DIRECTION: REVERSIBLE
COMMENT: When E. coli K-12 is grown on C-3 carbon sources both classes of aldolase are present. However the Class I enzyme is present only under these conditions. Therefore it is likely that the Class I enzyme is involved in gluconeogenesis and the class II enzyme in glycolysis. |CITS: [81000551]| The class I enzymes function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion. |CITS:[89193446]| They form a Schiff base betwen the E-amino group of a specific lysine residue in the active site and the carbonyl group of the substrate. This imine may be reduced by borohydride which therefore irreversibly inhibits class 1 aldolases in the presence of substrate. |CITS:[73229139]| The enzyme's activity was unaffected by EDTA, but it was inhibited by borohydride reduction in the presence of Fru-1,6-P2 or dihydroxyacetone phosphate. Like mammalian aldolases, it cleaved fructose 1-phosphate, albeit slowly and had a low Km for Fru-1,6-P2. Its fructose 1,6 bisphosphate cleavage activity was greatly enhanced by citrate, PEP, 2-oxoglutarate and sn-glycerol 3-phosphate. Aldolase I is very efficient at Fru-1,6-P2 cleavage when fully activated. Only a limited range of metabolites has been tested as possible activators. In contrast, its fructose 1-phosphate cleavage activity was unaffected by these compounds. The enhancement exhibited a strong dependence on pH. These novel kinetic properties do not seem to be shared by any other fructose 1,6 bisphosphate aldolase. In view of its unusual properties, it is unlikely that aldolase I from E.coli is closely related to the class-1 aldolases that have been detected in several other prokaryotes, or to the typical class I enzymes from eukaryote. |CITS: [78165652]|
NAME: fructose bisphosphate aldolase class I
CONTROLLED: biochemicalReaction295
CONTROLLER: physicalEntityParticipant281
XREF: publicationXref294

catalysis296
type: NamedIndividual
type: catalysis
DIRECTION: REVERSIBLE
SYNONYMS: TIM
COMMENT: The amino acid sequence around the active site is perfectly conserved in all known triose phosphate isomerases and can be used as a signature pattern for this type of enzyme.|CITS: [Prosite]|
SYNONYMS: phosphotriose isomerase
NAME: triose phosphate isomerase
SYNONYMS: triosephosphate isomerase
SYNONYMS: triosephosphate mutase
CONTROLLED: biochemicalReaction297
CONTROLLER: physicalEntityParticipant264

catalysis299
type: NamedIndividual
type: catalysis
COMMENT: Class II enzymes utilize a divalent metal ion to act as the electron sink at the active site in what appears to be an otherwise similar catalytic mechanism to Class I. |CITS: [89193446]| The metal ion in the active site varies, but several metals including zinc, cobalt, iron, nickel and manganese can form an active metallo-protein complex |CITS: [73229139]| In Crookes strain of E. coli it was found that the kinetic behavior is not typical of a class-II aldolase; the enzyme has no requirement for thiol compounds either for stability or activity, added K+ ions have no effect, and the high pH optimum of 9 is unusual for a class II enzyme. |CITS: [78165651]| Aldolase II is relatively insensitive to compounds that react with thiol groups.|CITS: [78165651]| It is strongly inhibited by metal-chelating agents and is reactivated by bivalent metal ions.|CITS: [73229139]| When E. coli K-12 is grown on C-3 carbon sources both classes of aldolase are present. However the Class I enzyme is present only under these conditions. Therefore the Class I enzyme is most likely involved in gluconeogenesis and the Class II enzyme with glycolysis. |CITS: [81000551]|
DIRECTION: REVERSIBLE
NAME: fructose bisphosphate aldolase class II
SYNONYMS: fructose-1,6-bisphosphate aldolase
SYNONYMS: fructose-1,6-bisphosphate triosephosphate lyase
CONTROLLED: biochemicalReaction295
CONTROLLER: physicalEntityParticipant289
XREF: publicationXref259
XREF: publicationXref274
XREF: publicationXref275

catalysis321
type: NamedIndividual
type: catalysis
COMMENT: 2-deoxyglucose-6-p is a known inhibitor in mammalian systems. E.coli cells with mutated pgi gene apparently utilize glucose primarily by the pentose phosphate pathway and to a lesser extent by the Entner-Duodoroff pathway. |CITS:[89364675]|
SYNONYMS: D-glucose-6-phosphate-ketol-isomerase
DIRECTION: REVERSIBLE
SYNONYMS: glucose-6-phosphate isomerase
NAME: phosphoglucose isomerase
CONTROLLED: biochemicalReaction260
CONTROLLER: physicalEntityParticipant323
XREF: publicationXref280
XREF: publicationXref322

catalysis55
type: NamedIndividual
type: catalysis
SYNONYMS: BPG-independent PGAM
SYNONYMS: D-phosphoglycerate 2,3-phosphomutase
COMMENT: E. coli contains three phosphoglycerate mutases. Two are 2,3-bisphosphoglycerate-dependent enzymes, encoded by the gpmA and gpmB genes. The third is a 2,3-bisphosphoglycerate-independent enzyme encoded by the pgmI gene. The two cofactor-dependent enzymes are similar in sequence while the cofactor-independent enzyme is unrelated. The cofactor-dependent enzymes have ten times higher specific activity compared to the cofactor-independent enzyme. |CITS: [99364512]|
SYNONYMS: PGAM, cofactor independent
DIRECTION: REVERSIBLE
SYNONYMS: iPGM
SYNONYMS: phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent
SYNONYMS: phosphoglycerate mutase, BPG-independent
NAME: phosphoglycerate mutase, cofactor independent
SYNONYMS: phosphoglycerate phosphomutase
SYNONYMS: phosphoglyceromutase
CONTROLLED: biochemicalReaction56
CONTROLLER: physicalEntityParticipant65
COFACTOR: physicalEntityParticipant71

catalysis73
type: NamedIndividual
type: catalysis
SYNONYMS: BPG-dependent PGAM1
SYNONYMS: D-phosphoglycerate 2,3-phosphomutase 1
COMMENT: E. coli contains three phosphoglycerate mutases. Two are 2,3-bisphosphoglyerate-dependent enzymes, encoded by the gpmA and gpmB genes. The third is a 2,3-bisphosphoglyerate-independent enzyme encoded by the pgmI gene. |CITS: [99364512]|
SYNONYMS: PGAM 1
DIRECTION: REVERSIBLE
NAME: phosphoglycerate mutase 1
SYNONYMS: phosphoglycerate phosphomutase 1
SYNONYMS: phosphoglyceromutase 1
CONTROLLED: biochemicalReaction56
CONTROLLER: physicalEntityParticipant74

catalysis83
type: NamedIndividual
type: catalysis
SYNONYMS: 2,3-diphospho-D-glycerate
SYNONYMS: 2-phospho-D glycerate phosphotransferase
SYNONYMS: 2-phospho-D-glycerate hydrolyase
SYNONYMS: 2-phosphoglycerate dehydratase
DIRECTION: REVERSIBLE
COMMENT: There are two active sites per active dimer. Functionally there are many similarities between E. coli enolase and other enolases studied. Thus the dependence on Mg for activity and the inhibition by fluoride in the presence of phosphate are quantitatively very similar for all enolases. Other catalytic parameters are also similar but minor quantitative distinctions indicate that E. coli enolase is more closely related to yeast enolase than to enolases from vertebrate muscle. The pH optimum of 8.1 is significantly higher than that for vertebrate enolases and even somewhat above that of yeast and plant enolases. |CITS:[72060411]|
NAME: enolase
SYNONYMS: phosphopyruvate hydratase
CONTROLLED: biochemicalReaction84
COFACTOR: physicalEntityParticipant5
CONTROLLER: physicalEntityParticipant95
XREF: publicationXref94

chemicalStructure112
type: NamedIndividual
type: chemicalStructure
STRUCTURE-DATA: <atom id="K+-atom1" elementType="K" x2="-1.0" y2="-1.0" formalCharge="1"/> <formula concise="K 1" formalCharge="1"/> 39.098 [K+1]
STRUCTURE-FORMAT: CML

chemicalStructure116
type: NamedIndividual
type: chemicalStructure
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STRUCTURE-FORMAT: CML

chemicalStructure135
type: NamedIndividual
type: chemicalStructure
STRUCTURE-DATA: <atom id="CA+2-atom1" elementType="CA" x2="-1.0" y2="-1.0" formalCharge="2"/> <formula concise="CA 1" formalCharge="2"/> 40.08 [Ca+2]
STRUCTURE-FORMAT: CML

chemicalStructure150
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type: chemicalStructure
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chemicalStructure176
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chemicalStructure179
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complex121
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type: complex
NAME: PKI-COMPLEX
COMMENT: Pyruvate kinase I and pyruvate kinase II differ in physical and chemical properties as well as in their kinetic behavior. Although the two forms are under independent genetic control they do coexist in a wide range of nutritional and metabolic states. The two forms are not interconvertible. Both show positive cooperative effects with respect to the substrate phosphoenolpyruvate.|CITS:[83114522]| The enzyme has a low nucleotide specificity and the 5'-diphosphates of guanosine, inosine, uridine and cytidine can all serve as phospho acceptors.|CITS: [90336973]| Form I from E coli unlike form II is remarkably stable. |CITS:[91315755]|
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant122

complex139
type: NamedIndividual
type: complex
NAME: PKII-CPLX
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant140

complex191
type: NamedIndividual
type: complex
COMMENT: E.coli is unusual in having two glyceraldehyde-3-phosphate dehydrogenases. The protein GAPDH-A has a sequence that is more similar to eukaryotic sequences than it is to prokaryotic types |CITS:[91087241]|. GapA is required for glycolysis, while Epd (GapB) is not |CITS: [9260967]|. GapA and Epd may be involved in production of pyridoxal 5'-phosphate (PLP) |CITS: [9696782]|.
NAME: GAPDH-A-CPLX
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant195
XREF: publicationXref170
XREF: publicationXref192
XREF: publicationXref193
XREF: publicationXref194

complex241
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type: complex
NAME: 6PFK-2-CPX
COMMENT: This enzyme is an isozyme with phosphofructokinase-1. The nucleotide sequences of the genes are not similar.|CITS: [85203917]|
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant242
XREF: publicationXref239
XREF: publicationXref243

complex265
type: NamedIndividual
type: complex
NAME: TPI
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant250

complex273
type: NamedIndividual
type: complex
NAME: FRUCBISALD-CLASSII
COMMENT: In relation to the Class I enzymes (primarily studied and found in eukaryotes) comparatively little is known about the class II enzymes. The Class II aldolases of Sacc. cer. and E. coli are the best characterized.|CITS: [89193446]| It resembles the typical class II aldolase from yeast in size and amino acid composition. This is a strong suggestion that they are related. |CITS:[78165651]| These less well studied aldolases are found both in the eukaryotic green algae and fungi, and in the prokaryotic blue-green algae and bacteria. |CITS:[78165651]| The gene pgk, encoding the enzyme phosphoglycerate kinase, was carried on plasmid pLC33-5 of the collection of Clarke and Carbon. It was also noted that E.coli cells tansformed with this plasmid exhibited raised levels of Class II fructose 1,6 bisphosphate aldolase activity, suggesting that the same plasmid might also carry the structural gene (fba) for this enzyme. |CITS: [89193446]|
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant276
XREF: publicationXref274
XREF: publicationXref275

complex282
type: NamedIndividual
type: complex
NAME: FRUCBISALD-CLASSI
COMMENT: The typical class I aldolases of plants and animals have been throroughly studied |CITS: [78165651]| Fructose-1,6-bisphosphate aldolases can be divided into two classes on the basis of their catalytic and structural properties. |CITS: [78165651]| Class I fructose 1,6 bisphosphate aldolases were once thought to be confined to eukaryotic organisms but have since been detected in several bacterial species. |CITS: [78165652]| The occurence of such an aldolase in bacteria was unexpected in light of the phylogenetic distribution of aldolases. |CITS: [73229139]| The enzymes of eukaryotes generally fall into Class I and are tetramers of identical polypeptide chains. |CITS: [89193446]| In earlier studies |CITS: [73229139]| it was thought that the class I E. coli aldolase was typical in that it was tetrameric with a mol. wt. of approx. 140K. In 1978 new purification techniques were used.The true aldolase 1 activity could be measured by using Fru-1,6-P2 that had been purified by chromatography on DEAE-cellulose to remove the fructose-6-phosphate. Using these methods the enzyme appeared to be larger than was previously supposed and may be a decamer with a mol. wt. of approx. 340,000. The size of aldolase 1 and the effect of cross-linking reagents on it, indicate that its structure must differ significantly from that of the typical tetrameric class-I enzymes from eukaryotes. |CITS: [78165652] [73229139]|
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant283

complex38
type: NamedIndividual
type: complex
NAME: 6PFK-1-CPX
COMMENT: This enzyme is an isozyme with phosphofructokinase-2. The nucleotide sequences of the genes are not similar |CITS: [85203917]|. The tetrameric species is the only one which can bind both substrates and effectors, and thus have both catalytic and regulatory properties. The C terminal end of the peptide is required for allosteric properties.|CITS: [90276415]| Crystal structures have been solved with and without activators and inhibitors. |CITS: [89342465], [89125622]|
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant39
XREF: publicationXref10
XREF: publicationXref11
XREF: publicationXref4
XREF: publicationXref8

complex75
type: NamedIndividual
type: complex
NAME: PHOSGLYCMUTASE
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant76

complex96
type: NamedIndividual
type: complex
NAME: ENOLASE-CPLX
COMMENT: The enzyme denatures in the absence of Mg. When E. coli enolase was treated with EDTA in attempts to remove all residual activity prior to the Mg activation studies, it was found that the enzyme was unstable in the absence of Mg and that substantial and irreversible loss of activity was observed after very short exposure of the enzyme to EDTA. |CITS:[72060411]|
ORGANISM: bioSource43
COMPONENTS: physicalEntityParticipant97

dataSource319
type: NamedIndividual
type: dataSource
NAME: EcoCyc Database (http://ecocyc.org)

modulation1
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION-NONALLOSTERIC
CONTROLLED: catalysis2
CONTROLLER: physicalEntityParticipant22

modulation104
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
CONTROLLED: catalysis83
CONTROLLER: physicalEntityParticipant105

modulation108
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
COMMENT: high concentrations of Mg+2 and ADP |CITS:[89228557]|
CONTROLLED: catalysis109
CONTROLLER: physicalEntityParticipant33

modulation132
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
COMMENT: An activator only at low Mg+2 and Ca+2 concentrations, otherwise it is an inhibitor. |CITS: [83282602]|
CONTROLLED: catalysis109
CONTROLLER: physicalEntityParticipant133

modulation136
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
COMMENT: high concentrations of Mg+2 and ADP |CITS:[89228557]|
CONTROLLED: catalysis109
CONTROLLER: physicalEntityParticipant133

modulation147
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
COMMENT: high concentrations of Mg+2 and ADP |CITS:[89228557]|
CONTROLLED: catalysis109
CONTROLLER: physicalEntityParticipant148

modulation152
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION-ALLOSTERIC
CONTROLLED: catalysis109
CONTROLLER: physicalEntityParticipant29

modulation153
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION-ALLOSTERIC
CONTROLLED: catalysis137
CONTROLLER: physicalEntityParticipant154

modulation158
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
COMMENT: Vanadate strongly inhibits the enzyme. |CITS: [99364512]|
CONTROLLED: catalysis73
CONTROLLER: physicalEntityParticipant159

modulation206
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis207
CONTROLLER: physicalEntityParticipant57

modulation215
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis207
CONTROLLER: physicalEntityParticipant33

modulation216
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis189
CONTROLLER: physicalEntityParticipant217
XREF: publicationXref220

modulation232
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION-ALLOSTERIC
CONTROLLED: catalysis2
CONTROLLER: physicalEntityParticipant233

modulation237
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
CONTROLLED: catalysis238
CONTROLLER: physicalEntityParticipant29
XREF: publicationXref244

modulation298
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
CONTROLLED: catalysis299
CONTROLLER: physicalEntityParticipant300

modulation302
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
CONTROLLED: catalysis293
CONTROLLER: physicalEntityParticipant303

modulation308
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION-ALLOSTERIC
CONTROLLED: catalysis2
CONTROLLER: physicalEntityParticipant16

modulation310
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis293
CONTROLLER: physicalEntityParticipant85

modulation311
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis293
CONTROLLER: physicalEntityParticipant312

modulation313
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
CONTROLLED: catalysis293
CONTROLLER: physicalEntityParticipant228

modulation314
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis293
CONTROLLER: physicalEntityParticipant315

modulation316
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION-ALLOSTERIC
CONTROLLED: catalysis2
CONTROLLER: physicalEntityParticipant85

modulation317
type: NamedIndividual
type: modulation
CONTROL-TYPE: INHIBITION
CONTROLLED: catalysis238
CONTROLLER: physicalEntityParticipant33
XREF: publicationXref239

modulation318
type: NamedIndividual
type: modulation
CONTROL-TYPE: ACTIVATION
CONTROLLED: catalysis2
CONTROLLER: physicalEntityParticipant154

openControlledVocabulary17
type: NamedIndividual
type: openControlledVocabulary
TERM: cytoplasm
XREF: unificationXref18

openControlledVocabulary40
type: NamedIndividual
type: openControlledVocabulary
TERM: cellular_component unknown
XREF: unificationXref41

pathway305
type: NamedIndividual
type: pathway
SYNONYMS: Embden-Meyerhof pathway
COMMENT: Pyruvate from glycolysis proceeds to the pyruvate dehydrogenase multienzyme complex, and the acetyl CoA produced then proceeds on to the superpathway of glyoxylate bypass and TCA.
AVAILABILITY: This pathway is freely available to all users and may be redistributed in whole or in part provided proper source attribution is made. See http://biocyc.org/open-reg.shtml for more information.
SYNONYMS: glucose degradation
NAME: glycolysis I
DATA-SOURCE: dataSource319
PATHWAY-COMPONENTS: pathwayStep107
PATHWAY-COMPONENTS: pathwayStep171
PATHWAY-COMPONENTS: pathwayStep204
PATHWAY-COMPONENTS: pathwayStep306
PATHWAY-COMPONENTS: pathwayStep307
PATHWAY-COMPONENTS: pathwayStep309
PATHWAY-COMPONENTS: pathwayStep320
PATHWAY-COMPONENTS: pathwayStep54
PATHWAY-COMPONENTS: pathwayStep82

physicalEntityParticipant105
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule106

physicalEntityParticipant110
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule111

physicalEntityParticipant114
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule115

physicalEntityParticipant122
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 4.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein123

physicalEntityParticipant133
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule134

physicalEntityParticipant140
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 4.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein141

physicalEntityParticipant148
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule149

physicalEntityParticipant154
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule155

physicalEntityParticipant159
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule160

physicalEntityParticipant16
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule19

physicalEntityParticipant173
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule174

physicalEntityParticipant177
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule178

physicalEntityParticipant180
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule181

physicalEntityParticipant184
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule185

physicalEntityParticipant188
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule51

physicalEntityParticipant195
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 4.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: protein196

physicalEntityParticipant217
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule218

physicalEntityParticipant22
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule23

physicalEntityParticipant228
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule229

physicalEntityParticipant233
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule234

physicalEntityParticipant242
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 2.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein221

physicalEntityParticipant250
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 2.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein251

physicalEntityParticipant26
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule27

physicalEntityParticipant261
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule262

physicalEntityParticipant276
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 2.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein277

physicalEntityParticipant283
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 10.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein284

physicalEntityParticipant29
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule30

physicalEntityParticipant300
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule301

physicalEntityParticipant303
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule304

physicalEntityParticipant312
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule247

physicalEntityParticipant315
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule268

physicalEntityParticipant33
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule34

physicalEntityParticipant39
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 4.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein42

physicalEntityParticipant5
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule6

physicalEntityParticipant57
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule58

physicalEntityParticipant61
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule62

physicalEntityParticipant71
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
PHYSICAL-ENTITY: smallMolecule72

physicalEntityParticipant76
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 2.0
CELLULAR-LOCATION: openControlledVocabulary40
PHYSICAL-ENTITY: protein77

physicalEntityParticipant85
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule86

physicalEntityParticipant90
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 1.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: smallMolecule91

physicalEntityParticipant97
type: NamedIndividual
type: physicalEntityParticipant
STOICHIOMETRIC-COEFFICIENT: 2.0
CELLULAR-LOCATION: openControlledVocabulary17
PHYSICAL-ENTITY: protein98

protein123
type: NamedIndividual
type: protein
SYNONYMS: B1676
SEQUENCE: MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVIEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLEFNNDNRKLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALTTNEKTAHQLVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVPSGTTNTASVHVL
SYNONYMS: PykF
COMMENT: Type I pyruvate kinase is made up of 522 amino acids. Neither type I nor II contains tryptophan. The two forms of the enzyme, I and II are different proteins.|CITS:[83114522]| Pyruvate kinase F was previously referred to as pyruvate kinase B, now as I |CITS:[84029179]| A free N-terminal amino acid can be detected in both forms of pyruvate kinase it corresponds to methionine for type I and serine for type II.|CITS:[83114522]| Comparison with the known primary structures shows that bacterial enzymes lack a substantial portion of the N-terminal sequence with respect to pyruvate kinases from vertebrates. |CITS:[91315755]|
NAME: pyruvate kinase I monomer
ORGANISM: bioSource43
XREF: relationshipXref131
XREF: unificationXref124
XREF: unificationXref125
XREF: unificationXref126
XREF: unificationXref127
XREF: unificationXref128
XREF: unificationXref129
XREF: unificationXref130

protein141
type: NamedIndividual
type: protein
SYNONYMS: B1854
SEQUENCE: MSRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAKLGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPADVVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKADIKTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCSQDAMDDIILASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDNVEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALYRGVTPVHFDSANDGVAAASEAVNLLRDKGYLMSGDLVIVTQGDVMSTVGSTNTTRILTVE
SYNONYMS: PykA
COMMENT: There are 2 genes, pykA and pykF, for 2 isozymes
NAME: pyruvate kinase II monomer
ORGANISM: bioSource43
XREF: relationshipXref142
XREF: unificationXref143
XREF: unificationXref144
XREF: unificationXref145
XREF: unificationXref146

protein163
type: NamedIndividual
type: protein
SYNONYMS: B4395
SYNONYMS: GpmB
SEQUENCE: MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVATRAKELGITHIISSDLGRTRRTAEIIAQACGCDIIFDSRLRELNMGVLEKRHIDSLTEEEENWRRQLVNGTVDGRIPEGESMQELSDRVNAALESCRDLPQGSRPLLVSHGIALGCLVSTILGLPAWAERRLRLRNCSISRVDYQESLWLASGWVVETAGDISHLDAPALDELQR
NAME: PGAM2-MONOMER
COMMENT: The enzyme has not been characterized and the subunit structure is unknown. However, phosphoglycerate mutase 1 is a homodimer.
SYNONYMS: YtjC
ORGANISM: bioSource43
XREF: relationshipXref164
XREF: unificationXref165
XREF: unificationXref166
XREF: unificationXref167
XREF: unificationXref168

protein196
type: NamedIndividual
type: protein
COMMENT: A higher degree of sequence homology exists between E.coli and eucaryotic enzymes than betwen E. coli and the thermophilic bacterial enzyme |CITS:[85257641]|. Mutant exhibits a growth defect and also exhibits increased aggregation and lysis that are rescued by high-salt media |CITS: [9260967]|. Regulation has been described |CITS: [12672900]|. The regulation of the fkpA, gapA, and hslT genes is affected by evolution under conditions of chronic heat stress |CITS: [12672900]|.
SYNONYMS: B1779
SYNONYMS: Gad
SYNONYMS: Gap1
SYNONYMS: GapA
SEQUENCE: MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK
NAME: glyceraldehyde 3-phosphate dehydrogenase-A monomer
ORGANISM: bioSource43
XREF: publicationXref170
XREF: publicationXref192
XREF: relationshipXref169
XREF: unificationXref197
XREF: unificationXref198
XREF: unificationXref199
XREF: unificationXref200
XREF: unificationXref201
XREF: unificationXref202

protein209
type: NamedIndividual
type: protein
SYNONYMS: B2926
SEQUENCE: MSVIKMTDLDLAGKRVFIRADLNVPVKDGKVTSDARIRASLPTIELALKQGAKVMVTSHLGRPTEGEYNEEFSLLPVVNYLKDKLSNPVRLVKDYLDGVDVAEGELVVLENVRFNKGEKKDDETLSKKYAALCDVFVMDAFGTAHRAQASTHGIGKFADVACAGPLLAAELDALGKALKEPARPMVAIVGGSKVSTKLTVLDSLSKIADQLIVGGGIANTFIAAQGHDVGKSLYEADLVDEAKRLLTTCNIPVPSDVRVATEFSETAPATLKSVNDVKADEQILDIGDASAQELAEILKNAKTILWNGPVGVFEFPNFRKGTEIVANAIADSEAFSIAGGGDTLAAIDLFGIADKISYISTGGGAFLEFVEGKVLPAVAMLEERAKK
NAME: PGK
SYNONYMS: Pgk
COMMENT: Phosphoglycerate kinase is one of the proteins induced by anaerobiosis. |CITS:[89306676]| The gene is transcribed from two promoters, one immediately in front of an upstream gene coding for a 38-kDa polypeptide of unknown function. The pgk gene was also found to show growth phase regulation. A structural determinant for glycerate 3-P kinase is located near serA. The map order is speB-pgk-serA-lysA-argA-eno-cysC.|CITS:[76195925]| Pgk has similarity to an Edwardsiella ictaluri protein |CITS: [12542086]|.
ORGANISM: bioSource43
XREF: relationshipXref214
XREF: unificationXref210
XREF: unificationXref211
XREF: unificationXref212
XREF: unificationXref213

protein221
type: NamedIndividual
type: protein
NAME: 6-phosphofructokinase-2 monomer
SYNONYMS: B1723
SEQUENCE: MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR
SYNONYMS: PfkB
ORGANISM: bioSource43
XREF: publicationXref222
XREF: relationshipXref223
XREF: unificationXref224
XREF: unificationXref225
XREF: unificationXref226

protein251
type: NamedIndividual
type: protein
SYNONYMS: B3919
SEQUENCE: MRHPLVMGNWKLNGSRHMVHELVSNLRKELAGVAGCAVAIAPPEMYIDMAKREAEGSHIMLGAQNVDLNLSGAFTGETSAAMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKADAFAVIVKAAEAAKQA
SYNONYMS: Tpi
SYNONYMS: TpiA
NAME: triose phosphate isomerase monomer
ORGANISM: bioSource43
XREF: relationshipXref258
XREF: unificationXref252
XREF: unificationXref253
XREF: unificationXref254
XREF: unificationXref255
XREF: unificationXref256
XREF: unificationXref257

protein277
type: NamedIndividual
type: protein
SYNONYMS: Ald
SYNONYMS: B2925
SYNONYMS: Fba
SYNONYMS: FbaA
SYNONYMS: Fda
SEQUENCE: MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL
COMMENT: The amino acid sequence of the E.coli Class II fructose-1,6-bisphosphate aldolase inferred from the DNA sequence of the fda gene is the first primary structure of a Class II aldolase to be established. There is no immediately apparent sequence homology with any of the Class I fructose-1,6-bisphosphate aldolases which have been widely studied. |CITS:[89193446]| An fda mutant exhibits a heat-sensitive defect in rRNA transcription that is elicited via altered abundance of ppGpp and of initiating NTPs |CITS: [14526031]|. Fda has similarity to an Edwardsiella ictaluri protein that provokes an immune response in catfish |CITS: [12542086]|.
NAME: fructose bisphosphate aldolase monomer
ORGANISM: bioSource43
XREF: relationshipXref266
XREF: unificationXref245
XREF: unificationXref246
XREF: unificationXref267
XREF: unificationXref278
XREF: unificationXref279

protein284
type: NamedIndividual
type: protein
SYNONYMS: B2097
SYNONYMS: DhnA
SYNONYMS: FbaB
SEQUENCE: MIARKRRARTIHSRYPIGIYGSIVMTDIAQLLGKDADNLLQHRCMTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHSAGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGVDYHVSADLTGQANHLAATIGADIVKQKMAENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILGRKAFKKSMADGVKLINAVQDVYLDSKITIA
NAME: fructose bisphosphate aldolase monomer
ORGANISM: bioSource43
XREF: relationshipXref285
XREF: unificationXref286
XREF: unificationXref287
XREF: unificationXref288

protein290
type: NamedIndividual
type: protein
SYNONYMS: B4025
SEQUENCE: MKNINPTQTAAWQALQKHFDEMKDVTIADLFAKDGDRFSKFSATFDDQMLVDYSKNRITEETLAKLQDLAKECDLAGAIKSMFSGEKINRTENRAVLHVALRNRSNTPILVDGKDVMPEVNAVLEKMKTFSEAIISGEWKGYTGKAITDVVNIGIGGSDLGPYMVTEALRPYKNHLNMHFVSNVDGTHIAEVLKKVNPETTLFLVASKTFTTQETMTNAHSARDWFLKAAGDEKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIVLSIGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGNVVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKMVPCDFIAPAITHNPLSDHHQKLLSNFFAQTEALAFGKSREVVEQEYRDQGKDPATLDYVVPFKVFEGNRPTNSILLREITPFSLGALIALYEHKIFTQGVILNIFTFDQWGVELGKQLANRILPELKDDKEISSHDSSTNGLINRYKAWRG
NAME: PGLUCISOM
SYNONYMS: Pgi
COMMENT: phosphoglucose isomerase is found primarily in the cytoplasm
ORGANISM: bioSource43
XREF: publicationXref280
XREF: relationshipXref291
XREF: unificationXref271
XREF: unificationXref272
XREF: unificationXref292

protein42
type: NamedIndividual
type: protein
NAME: 6-phosphofructokinase-1 monomer
SYNONYMS: B3916
SEQUENCE: MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY
SYNONYMS: PfkA
ORGANISM: bioSource43
XREF: relationshipXref46
XREF: unificationXref45
XREF: unificationXref47
XREF: unificationXref48
XREF: unificationXref49
XREF: unificationXref50

protein66
type: NamedIndividual
type: protein
SYNONYMS: B3612
SYNONYMS: GpmC
SYNONYMS: GpmI
SYNONYMS: GpmM
SEQUENCE: MLVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIRAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAVEGGKLSDIAPTMLSLMGMEIPQEMTGKPLFIVE
NAME: PGMI-MONOMER
SYNONYMS: PgmI
SYNONYMS: YibO
ORGANISM: bioSource43
XREF: relationshipXref67
XREF: unificationXref68
XREF: unificationXref69
XREF: unificationXref70

protein77
type: NamedIndividual
type: protein
SYNONYMS: B0755
SYNONYMS: Gpm
NAME: GpmA
SYNONYMS: GpmA
SEQUENCE: MAVTKLVLVRHGESQWNKENRFTGWYDVDLSEKGVSEAKAAGKLLKEEGYSFDFAYTSVLKRAIHTLWNVLDELDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPELTKDDERYPGHDPRYAKLSEKELPLTESLALTIDRVIPYWNETILPRMKSGERVIIAAHGNSLRALVKYLDNMSEEEILELNIPTGVPLVYEFDENFKPLKRYYLGNADEIAAKAAAVANQGKAK
SYNONYMS: Pgm
SYNONYMS: PgmA
COMMENT: Regulation has been described |CITS: [11101675]|. Transcription is regulated by Fur |CITS: [11101675]|.
ORGANISM: bioSource43
XREF: unificationXref78
XREF: unificationXref79
XREF: unificationXref80
XREF: unificationXref81

protein98
type: NamedIndividual
type: protein
SYNONYMS: B2779
SYNONYMS: Eno
NAME: Eno
SEQUENCE: MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTENKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGEKAPYNGRKEIKGQA
ORGANISM: bioSource43
XREF: relationshipXref102
XREF: unificationXref100
XREF: unificationXref101
XREF: unificationXref103
XREF: unificationXref99

publicationXref10
type: NamedIndividual
type: publicationXref
YEAR: 1988
ID: 2975709
TITLE: Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products.
AUTHORS: Evans PR
SOURCE: J Mol Biol 1988;204(4);973-94
DB: PubMed
AUTHORS: Shirakihara Y

publicationXref11
type: NamedIndividual
type: publicationXref
YEAR: 1990
ID: 2140983
SOURCE: Eur J Biochem 1990;189(3);487-92
AUTHORS: Garel JR
DB: PubMed
TITLE: Role of the C-terminal region in the allosteric properties of Escherichia coli phosphofructokinase-1.
AUTHORS: Serre MC

publicationXref12
type: NamedIndividual
type: publicationXref
ID: 1832014
YEAR: 1991
AUTHORS: Berger SA
SOURCE: Biochemistry 1991;30(34);8477-80
AUTHORS: Evans PR
DB: PubMed
TITLE: Steady-state fluorescence of Escherichia coli phosphofructokinase reveals a regulatory role for ATP.

publicationXref14
type: NamedIndividual
type: publicationXref
TITLE: Biochemistry
AUTHORS: Stryer L
SOURCE: WH Freeman and Co., 3rd edition, New York, 1988

publicationXref15
type: NamedIndividual
type: publicationXref
ID: 153704
YEAR: 1979
SOURCE: Adv Enzymol Relat Areas Mol Biol 1979;48;193-244
TITLE: Phosphofructokinase.
DB: PubMed
AUTHORS: Uyeda K

publicationXref170
type: NamedIndividual
type: publicationXref
YEAR: 1997
ID: 9260967
AUTHORS: Boschi-Muller S
AUTHORS: Branlant G
TITLE: Characterization of Escherichia coli strains with gapA and gapB genes deleted.
SOURCE: J Bacteriol 1997;179(16);5218-21
DB: PubMed
AUTHORS: Seta FD
AUTHORS: Vignais ML

publicationXref192
type: NamedIndividual
type: publicationXref
YEAR: 1985
ID: 2990926
AUTHORS: Branlant C
AUTHORS: Branlant G
SOURCE: Eur J Biochem 1985;150(1);61-6
TITLE: Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase.
DB: PubMed

publicationXref193
type: NamedIndividual
type: publicationXref
YEAR: 1998
ID: 9696782
TITLE: Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12.
SOURCE: J Bacteriol 1998;180(16);4294-9
AUTHORS: Man TK
DB: PubMed
AUTHORS: Winkler ME
AUTHORS: Yang Y
AUTHORS: Zhao G

publicationXref194
type: NamedIndividual
type: publicationXref
YEAR: 1990
ID: 2124629
TITLE: A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote.
AUTHORS: Alberro MR
AUTHORS: Anderson KL
AUTHORS: Doolittle RF
AUTHORS: Feng DF
SOURCE: J Mol Evol 1990;31(5);383-8
DB: PubMed

publicationXref203
type: NamedIndividual
type: publicationXref
TITLE: Oxidation-Reduction, Part C
SOURCE: The Enzymes, Vol.XIII Academic Press, New York 1976;3rd Edition

publicationXref220
type: NamedIndividual
type: publicationXref
YEAR: 1995
ID: 7751290
AUTHORS: Bharani N
TITLE: Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.
SOURCE: J Bacteriol 1995;177(10);2804-12
AUTHORS: Pease AJ
DB: PubMed
AUTHORS: Winkler ME
AUTHORS: Zhao G

publicationXref222
type: NamedIndividual
type: publicationXref
YEAR: 1984
ID: 6235149
AUTHORS: Daldal F
SOURCE: Gene 1984;28(3);337-42
TITLE: Nucleotide sequence of gene pfkB encoding the minor phosphofructokinase of Escherichia coli K-12.
DB: PubMed

publicationXref239
type: NamedIndividual
type: publicationXref
YEAR: 1981
ID: 6456900
AUTHORS: Buc H
SOURCE: Eur J Biochem 1981;117(3);569-74
AUTHORS: Kotlarz D
DB: PubMed
TITLE: Regulatory properties of phosphofructokinase 2 from Escherichia coli.

publicationXref243
type: NamedIndividual
type: publicationXref
YEAR: 1985
ID: 3158524
SOURCE: Eur J Biochem 1985;149(2);363-73
AUTHORS: Evans PR
AUTHORS: Hellinga HW
TITLE: Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase.
DB: PubMed

publicationXref244
type: NamedIndividual
type: publicationXref
ID: 149128
YEAR: 1978
AUTHORS: Babul J
SOURCE: J Biol Chem 1978;253(12);4350-5
TITLE: Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme.
DB: PubMed

publicationXref259
type: NamedIndividual
type: publicationXref
YEAR: 1973
ID: 4198624
SOURCE: Biochem J 1973;131(4);833-41
AUTHORS: Perham RN
DB: PubMed
TITLE: Purification and characterization of two fructose diphosphate aldolases from Escherichia coli (Crookes' strain).
AUTHORS: Stribling D

publicationXref274
type: NamedIndividual
type: publicationXref
YEAR: 1989
ID: 2649077
AUTHORS: Alefounder PR
AUTHORS: Baldwin SA
SOURCE: Biochem J 1989;257(2);529-34
TITLE: Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli.
AUTHORS: Perham RN
DB: PubMed
AUTHORS: Short NJ

publicationXref275
type: NamedIndividual
type: publicationXref
YEAR: 1978
ID: 417719
AUTHORS: Baldwin SA
SOURCE: Biochem J 1978;169(3);633-41
AUTHORS: Perham RN
DB: PubMed
TITLE: Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain).
AUTHORS: Stribling D

publicationXref280
type: NamedIndividual
type: publicationXref
YEAR: 1989
ID: 2549364
AUTHORS: Froman BE
AUTHORS: Gottlieb LD
TITLE: Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli.
SOURCE: Mol Gen Genet 1989;217(1);126-31
DB: PubMed
AUTHORS: Tait RC

publicationXref294
type: NamedIndividual
type: publicationXref
YEAR: 1998
ID: 9531482
AUTHORS: Ashcroft AE
AUTHORS: Berry A
SOURCE: Biochem J 1998;331 ( Pt 2);437-45
AUTHORS: Howlett GJ
DB: PubMed
TITLE: The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase.
AUTHORS: Thomson GJ

publicationXref3
type: NamedIndividual
type: publicationXref
YEAR: 1989
ID: 2531001
SOURCE: Biochemistry 1989;28(17);6836-41
AUTHORS: Bras GL
AUTHORS: Deville-Bonne D
AUTHORS: Garel JR
DB: PubMed
AUTHORS: Teschner W
TITLE: Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli.

publicationXref322
type: NamedIndividual
type: publicationXref
SOURCE: BBA 1964;92:378-387
AUTHORS: Endresen A
TITLE: Intracellular pH effect upon phosphoglucose isomerase in Escherichia coli
AUTHORS: Klungsoyr L

publicationXref4
type: NamedIndividual
type: publicationXref
ID: 1828369
YEAR: 1991
SOURCE: Biochemistry 1991;30(23);5750-4
AUTHORS: Bourgain F
AUTHORS: Deville-Bonne D
AUTHORS: Garel JR
DB: PubMed
TITLE: pH dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coli.

publicationXref8
type: NamedIndividual
type: publicationXref
YEAR: 1989
ID: 2527305
TITLE: Crystal structure of unliganded phosphofructokinase from Escherichia coli.
AUTHORS: Evans PR
SOURCE: J Mol Biol 1989;207(4);805-21
DB: PubMed
AUTHORS: Rypniewski WR

publicationXref9
type: NamedIndividual
type: publicationXref
ID: 1531298
YEAR: 1992
TITLE: A conformational transition involved in antagonistic substrate binding to the allosteric phosphofructokinase from Escherichia coli.
SOURCE: Biochemistry 1992;31(6);1695-700
AUTHORS: Deville-Bonne D
AUTHORS: Garel JR
DB: PubMed

publicationXref94
type: NamedIndividual
type: publicationXref
YEAR: 1971
ID: 4942326
SOURCE: J Biol Chem 1971;246(22);6797-802
DB: PubMed
AUTHORS: Spring TG
TITLE: The purification and characterization of Escherichia coli enolase.
AUTHORS: Wold F

relationshipXref102
type: NamedIndividual
type: relationshipXref
ID: ENO-MONOMER
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog

relationshipXref131
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: PYKF-MONOMER

relationshipXref142
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: PYKA-MONOMER

relationshipXref164
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
ID: GPMB-MONOMER
RELATIONSHIP-TYPE: Ortholog

relationshipXref169
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
ID: GAPA-MONOMER
RELATIONSHIP-TYPE: Ortholog

relationshipXref214
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
ID: G7E-3-MONOMER
RELATIONSHIP-TYPE: Ortholog

relationshipXref223
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: PFKB-MONOMER

relationshipXref258
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: TPIA-MONOMER

relationshipXref266
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
ID: FBA-MONOMER
RELATIONSHIP-TYPE: Ortholog

relationshipXref285
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: Z3260-MONOMER

relationshipXref291
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: PGI-MONOMER

relationshipXref46
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: PFKA-MONOMER

relationshipXref67
type: NamedIndividual
type: relationshipXref
DB: EcoO157Cyc
RELATIONSHIP-TYPE: Ortholog
ID: YIBO-MONOMER

smallMolecule106
type: NamedIndividual
type: smallMolecule
SYNONYMS: F
NAME: F-
SYNONYMS: fluoride
SYNONYMS: fluoride ion

smallMolecule111
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 39.098
NAME: K+
SYNONYMS: potassium ion
STRUCTURE: chemicalStructure112

smallMolecule115
type: NamedIndividual
type: smallMolecule
SYNONYMS: 2-oxo-propionic acid
SYNONYMS: 2-oxopropanoate
SYNONYMS: 2-oxopropanoic acid
MOLECULAR-WEIGHT: 88.063
SYNONYMS: BTS
SYNONYMS: acetylformic acid
SYNONYMS: alpha-ketopropionic acid
SYNONYMS: pyroracemic acid
NAME: pyruvate
SYNONYMS: pyruvic acid
STRUCTURE: chemicalStructure116
XREF: unificationXref117
XREF: unificationXref118
XREF: unificationXref119

smallMolecule134
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 40.08
NAME: Ca2+
SYNONYMS: Ca++
SYNONYMS: Ca+2
SYNONYMS: calcium ion
STRUCTURE: chemicalStructure135

smallMolecule149
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 867.608
SYNONYMS: suc-co-A
SYNONYMS: suc-coa
SYNONYMS: succ-CoA
SYNONYMS: succ-S-CoA
SYNONYMS: succ-S-coenzyme-A
SYNONYMS: succ-coenzyme-A
NAME: succinyl-CoA
SYNONYMS: succinyl-S-CoA
SYNONYMS: succinyl-S-coenzyme-A
SYNONYMS: succinylcoenzyme-A
STRUCTURE: chemicalStructure150
XREF: unificationXref151

smallMolecule155
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 347.224
SYNONYMS: A
NAME: AMP
SYNONYMS: adenosine-5'-phosphate
SYNONYMS: adenosine-monophosphate
SYNONYMS: adenosine-phosphate
SYNONYMS: adenylate
SYNONYMS: adenylic acid
STRUCTURE: chemicalStructure157
XREF: unificationXref156

smallMolecule160
type: NamedIndividual
type: smallMolecule
NAME: vanadate

smallMolecule174
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 94.971
SYNONYMS: HPO42-
SYNONYMS: PO43-
SYNONYMS: Pi
SYNONYMS: inorganic phosphate
SYNONYMS: orthophosphate
NAME: phosphate
SYNONYMS: phosphate-inorganic
STRUCTURE: chemicalStructure176
XREF: unificationXref175

smallMolecule178
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 665.446
SYNONYMS: DPNH
SYNONYMS: NAD-reduced
NAME: NADH
SYNONYMS: NADH+H+
SYNONYMS: NADH2
SYNONYMS: dihydrodiphosphopyridine nucleotide
SYNONYMS: dihydronicotinamide adenine dinucleotide
SYNONYMS: diphosphopyridine nucleotide reduced
SYNONYMS: nicotinamide adenine dinucleotide reduced
STRUCTURE: chemicalStructure179

smallMolecule181
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 170.058
SYNONYMS: 3-phosphoglyceraldehyde
SYNONYMS: D-glyceraldehyde-3-P
SYNONYMS: D-glyceraldehyde-3-phosphate
SYNONYMS: gap
SYNONYMS: glyceraldehyde-3-P
NAME: glyceraldehyde-3-phosphate
SYNONYMS: glyceraldehyde-P
SYNONYMS: glyceraldehyde-phosphate
STRUCTURE: chemicalStructure183
XREF: unificationXref182

smallMolecule185
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 663.43
SYNONYMS: DPN
SYNONYMS: DPN+
SYNONYMS: DPN-ox
NAME: NAD
SYNONYMS: NAD+
SYNONYMS: NAD-ox
SYNONYMS: NAD-oxidized
SYNONYMS: coenzyme I
SYNONYMS: diphosphopyridine nucleotide
SYNONYMS: diphosphopyridine nucleotide oxidized
SYNONYMS: nicotinamide adenine dinucleotide
SYNONYMS: nicotinamide adenine dinucleotide oxidized
STRUCTURE: chemicalStructure186
XREF: unificationXref187

smallMolecule19
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 427.203
NAME: ADP
SYNONYMS: adenosine 5'-pyrophosphate
SYNONYMS: adenosine pyrophosphate
SYNONYMS: adenosine-5'-diphosphate
SYNONYMS: adenosine-5-diphosphate
SYNONYMS: adenosine-diphosphate
STRUCTURE: chemicalStructure20
XREF: unificationXref21

smallMolecule218
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 138.919
SYNONYMS: AsO43-
NAME: arsenate
SYNONYMS: inorganic arsenate
SYNONYMS: orthoarsenate
STRUCTURE: chemicalStructure219

smallMolecule229
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 170.058
SYNONYMS: DHAP
SYNONYMS: di-OH-acetone-P
NAME: dihydroxy-acetone-phosphate
SYNONYMS: dihydroxyacetone 3-phosphate
SYNONYMS: dihydroxyacetone-P
SYNONYMS: dihydroxyacetone-phosphate
SYNONYMS: glycerone-phosphate
STRUCTURE: chemicalStructure230
XREF: unificationXref231

smallMolecule23
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 260.137
SYNONYMS: A-D-fructose-6-P
SYNONYMS: D-fructose-6-P
SYNONYMS: D-fructose-6-phosphate
SYNONYMS: fru-6-P
SYNONYMS: fruc6p
SYNONYMS: fructose-6-P
NAME: fructose-6-phosphate
SYNONYMS: fructose-6P
STRUCTURE: chemicalStructure24
XREF: unificationXref25

smallMolecule234
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 443.203
NAME: GDP
SYNONYMS: guanosine-5'-diphosphate
SYNONYMS: guanosine-diphosphate
SYNONYMS: ppG
STRUCTURE: chemicalStructure236
XREF: unificationXref235

smallMolecule247
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 192.125
SYNONYMS: 2-hydroxy-1,2,3-propanetricarboxylic acid
SYNONYMS: cit
SYNONYMS: citr
NAME: citrate
SYNONYMS: citric acid
STRUCTURE: chemicalStructure248
XREF: unificationXref249

smallMolecule262
type: NamedIndividual
type: smallMolecule
SYNONYMS: α-D-glucose-6-P
SYNONYMS: α-D-glucose-6-phosphate
MOLECULAR-WEIGHT: 260.137
SYNONYMS: D-glucose-6-P
SYNONYMS: D-glucose-6-phosphate
SYNONYMS: glucose-6-P
NAME: glucose-6-phosphate
STRUCTURE: chemicalStructure263
XREF: unificationXref227

smallMolecule268
type: NamedIndividual
type: smallMolecule
SYNONYMS: α-glycerophosphate
MOLECULAR-WEIGHT: 172.074
SYNONYMS: D-glycerol-3-phosphate
SYNONYMS: glycerol-3-P
NAME: glycerol-3-phosphate
SYNONYMS: sn-glycerol-3-phosphate
STRUCTURE: chemicalStructure269
XREF: unificationXref270

smallMolecule27
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 1.008
SYNONYMS: H
NAME: H+
SYNONYMS: hydrogen ion
SYNONYMS: proton
STRUCTURE: chemicalStructure28

smallMolecule30
type: NamedIndividual
type: smallMolecule
SYNONYMS: α-D-fructose-1,6-diphosphate
MOLECULAR-WEIGHT: 340.117
SYNONYMS: D-fructose-1,6-bisphosphate
SYNONYMS: D-fructose-1,6-diphosphate
NAME: fructose-1,6-bisphosphate
SYNONYMS: fructose-1,6-diphosphate
STRUCTURE: chemicalStructure32
XREF: unificationXref31

smallMolecule301
type: NamedIndividual
type: smallMolecule
NAME: EDTA

smallMolecule304
type: NamedIndividual
type: smallMolecule
NAME: BOROHYDRIDE

smallMolecule34
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 507.183
NAME: ATP
SYNONYMS: adenosine-5'-triphosphate
SYNONYMS: adenosine-triphosphate
SYNONYMS: adenylpyrophosphate
STRUCTURE: chemicalStructure35
XREF: unificationXref36

smallMolecule51
type: NamedIndividual
type: smallMolecule
SYNONYMS: 1,3-biphosphoglycerate
SYNONYMS: 1,3-bis-phosphoglycerate
SYNONYMS: 1,3-diphosphateglycerate
SYNONYMS: 1,3-diphosphoglycerate
SYNONYMS: 13-dpg
MOLECULAR-WEIGHT: 266.038
SYNONYMS: 3-P-glyceroyl-P
NAME: 3-phospho-D-glyceroyl-phosphate
SYNONYMS: 3-phosphoglyceroyl-P
SYNONYMS: 3-phosphoglyceroyl-phosphate
SYNONYMS: P-glyceroyl-P
SYNONYMS: dpg
SYNONYMS: glycerate 1,3-biphosphate
SYNONYMS: glycerate 1,3-diphosphate
SYNONYMS: phosphoglyceroyl-P
STRUCTURE: chemicalStructure53
XREF: unificationXref52

smallMolecule58
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 186.058
SYNONYMS: 3-P-D-glycerate
SYNONYMS: 3-P-glycerate
SYNONYMS: 3-pg
SYNONYMS: 3-phospho-(R)-glycerate
SYNONYMS: 3-phospho-D-glycerate
SYNONYMS: 3-phospho-glyceric acid
NAME: 3-phosphoglycerate
SYNONYMS: D-Glycerate 3-phosphate
SYNONYMS: g3p
SYNONYMS: glycerate 3-phosphate
SYNONYMS: glycerate-3-P
STRUCTURE: chemicalStructure60
XREF: unificationXref59

smallMolecule6
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 24.305
NAME: Mg2+
SYNONYMS: Mg++
SYNONYMS: Mg+2
SYNONYMS: magnesium ion
STRUCTURE: chemicalStructure7

smallMolecule62
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 186.058
SYNONYMS: 2-P-D-glycerate
SYNONYMS: 2-P-glycerate
SYNONYMS: 2-pg
SYNONYMS: 2-phospho-D-glycerate
NAME: 2-phosphoglycerate
SYNONYMS: 2-phosphoglyceric acid
SYNONYMS: D-Glycerate 2-phosphate
SYNONYMS: glycerate 2-phosphate
STRUCTURE: chemicalStructure63
XREF: unificationXref64

smallMolecule72
type: NamedIndividual
type: smallMolecule
NAME: Mn2+
SYNONYMS: Mn++
SYNONYMS: Mn+2
SYNONYMS: manganese ion

smallMolecule86
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 168.043
SYNONYMS: P-enol-pyr
SYNONYMS: P-enol-pyruvate
SYNONYMS: PEP
NAME: phosphoenolpyruvate
STRUCTURE: chemicalStructure88
XREF: unificationXref87
XREF: unificationXref89

smallMolecule91
type: NamedIndividual
type: smallMolecule
MOLECULAR-WEIGHT: 18.015
SYNONYMS: H20
NAME: H2O
SYNONYMS: hydrogen oxide
SYNONYMS: water
STRUCTURE: chemicalStructure93
XREF: unificationXref92

unificationXref100
type: NamedIndividual
type: unificationXref
ID: P08324
DB: SWISS-MODEL

unificationXref101
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b2779

unificationXref103
type: NamedIndividual
type: unificationXref
ID: NP_417259
DB: RefSeq

unificationXref117
type: NamedIndividual
type: unificationXref
DB: UMBBD
ID: c0159

unificationXref118
type: NamedIndividual
type: unificationXref
ID: 127-17-3
DB: CAS

unificationXref119
type: NamedIndividual
type: unificationXref
DB: LIGAND
ID: c00022

unificationXref124
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b1676

unificationXref125
type: NamedIndividual
type: unificationXref
ID: P14178
DB: SWISS-PROT

unificationXref126
type: NamedIndividual
type: unificationXref
ID: 1E0T
DB: PDB

unificationXref127
type: NamedIndividual
type: unificationXref
ID: NP_416191
DB: RefSeq

unificationXref128
type: NamedIndividual
type: unificationXref
ID: P14178
DB: SWISS-MODEL

unificationXref129
type: NamedIndividual
type: unificationXref
ID: 1E0U
DB: PDB

unificationXref130
type: NamedIndividual
type: unificationXref
ID: 1PKY
DB: PDB

unificationXref143
type: NamedIndividual
type: unificationXref
ID: NP_416368
DB: RefSeq

unificationXref144
type: NamedIndividual
type: unificationXref
ID: P21599
DB: SWISS-PROT

unificationXref145
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b1854

unificationXref146
type: NamedIndividual
type: unificationXref
ID: P21599
DB: SWISS-MODEL

unificationXref151
type: NamedIndividual
type: unificationXref
ID: 604-98-8
DB: CAS

unificationXref156
type: NamedIndividual
type: unificationXref
ID: 61-19-8
DB: CAS

unificationXref165
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b4395

unificationXref166
type: NamedIndividual
type: unificationXref
ID: P36942
DB: SWISS-PROT

unificationXref167
type: NamedIndividual
type: unificationXref
ID: NP_418812
DB: RefSeq

unificationXref168
type: NamedIndividual
type: unificationXref
ID: P36942
DB: SWISS-MODEL

unificationXref175
type: NamedIndividual
type: unificationXref
ID: 14265-44-2
DB: CAS

unificationXref18
type: NamedIndividual
type: unificationXref
DB: GO
ID: GO:0005737

unificationXref182
type: NamedIndividual
type: unificationXref
ID: 142-10-9
DB: CAS

unificationXref187
type: NamedIndividual
type: unificationXref
ID: 53-84-9
DB: CAS

unificationXref197
type: NamedIndividual
type: unificationXref
ID: NP_416293
DB: RefSeq

unificationXref198
type: NamedIndividual
type: unificationXref
ID: P06977
DB: SWISS-MODEL

unificationXref199
type: NamedIndividual
type: unificationXref
ID: 1GAD
DB: PDB

unificationXref200
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b1779

unificationXref201
type: NamedIndividual
type: unificationXref
ID: 1GAE
DB: PDB

unificationXref202
type: NamedIndividual
type: unificationXref
ID: P06977
DB: SWISS-PROT

unificationXref21
type: NamedIndividual
type: unificationXref
ID: 58-64-0
DB: CAS

unificationXref210
type: NamedIndividual
type: unificationXref
ID: P11665
DB: SWISS-PROT

unificationXref211
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b2926

unificationXref212
type: NamedIndividual
type: unificationXref
ID: NP_417401
DB: RefSeq

unificationXref213
type: NamedIndividual
type: unificationXref
ID: P11665
DB: SWISS-MODEL

unificationXref224
type: NamedIndividual
type: unificationXref
ID: NP_416237
DB: RefSeq

unificationXref225
type: NamedIndividual
type: unificationXref
ID: P06999
DB: SWISS-PROT

unificationXref226
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b1723

unificationXref227
type: NamedIndividual
type: unificationXref
ID: 56-73-5
DB: CAS

unificationXref231
type: NamedIndividual
type: unificationXref
ID: 57-04-5
DB: CAS

unificationXref235
type: NamedIndividual
type: unificationXref
ID: 146-91-8
DB: CAS

unificationXref245
type: NamedIndividual
type: unificationXref
ID: NP_417400
DB: RefSeq

unificationXref246
type: NamedIndividual
type: unificationXref
ID: 1DOS
DB: PDB

unificationXref249
type: NamedIndividual
type: unificationXref
ID: 77-92-9
DB: CAS

unificationXref25
type: NamedIndividual
type: unificationXref
ID: 643-13-0
DB: CAS

unificationXref252
type: NamedIndividual
type: unificationXref
ID: 1TMH
DB: PDB

unificationXref253
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b3919

unificationXref254
type: NamedIndividual
type: unificationXref
ID: 1TRE
DB: PDB

unificationXref255
type: NamedIndividual
type: unificationXref
ID: P04790
DB: SWISS-PROT

unificationXref256
type: NamedIndividual
type: unificationXref
ID: NP_418354
DB: RefSeq

unificationXref257
type: NamedIndividual
type: unificationXref
ID: P04790
DB: SWISS-MODEL

unificationXref267
type: NamedIndividual
type: unificationXref
ID: 1ZEN
DB: PDB

unificationXref270
type: NamedIndividual
type: unificationXref
ID: 57-03-4
DB: CAS

unificationXref271
type: NamedIndividual
type: unificationXref
ID: P11537
DB: SWISS-PROT

unificationXref272
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b4025

unificationXref278
type: NamedIndividual
type: unificationXref
ID: P11604
DB: SWISS-PROT

unificationXref279
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b2925

unificationXref286
type: NamedIndividual
type: unificationXref
ID: NP_416600
DB: RefSeq

unificationXref287
type: NamedIndividual
type: unificationXref
ID: P71295
DB: SWISS-PROT

unificationXref288
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b2097

unificationXref292
type: NamedIndividual
type: unificationXref
ID: NP_418449
DB: RefSeq

unificationXref31
type: NamedIndividual
type: unificationXref
ID: 488-69-7
DB: CAS

unificationXref36
type: NamedIndividual
type: unificationXref
ID: 56-65-5
DB: CAS

unificationXref41
type: NamedIndividual
type: unificationXref
DB: GO
ID: GO:0008372

unificationXref44
type: NamedIndividual
type: unificationXref
ID: 83333
COMMENT: Escherichia coli K-12
DB: taxon

unificationXref45
type: NamedIndividual
type: unificationXref
ID: P06998
DB: SWISS-PROT

unificationXref47
type: NamedIndividual
type: unificationXref
ID: 2PFK
DB: PDB

unificationXref48
type: NamedIndividual
type: unificationXref
ID: NP_418351
DB: RefSeq

unificationXref49
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b3916

unificationXref50
type: NamedIndividual
type: unificationXref
ID: P06998
DB: SWISS-MODEL

unificationXref52
type: NamedIndividual
type: unificationXref
ID: 1981-49-3
DB: CAS

unificationXref59
type: NamedIndividual
type: unificationXref
ID: 820-11-1
DB: CAS

unificationXref64
type: NamedIndividual
type: unificationXref
ID: 2553-59-5
DB: CAS

unificationXref68
type: NamedIndividual
type: unificationXref
ID: P37689
DB: SWISS-PROT

unificationXref69
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b3612

unificationXref70
type: NamedIndividual
type: unificationXref
ID: NP_418069
DB: RefSeq

unificationXref78
type: NamedIndividual
type: unificationXref
ID: P31217
DB: SWISS-PROT

unificationXref79
type: NamedIndividual
type: unificationXref
ID: P31217
DB: SWISS-MODEL

unificationXref80
type: NamedIndividual
type: unificationXref
DB: PIR
ID: b0755

unificationXref81
type: NamedIndividual
type: unificationXref
ID: NP_415276
DB: RefSeq

unificationXref87
type: NamedIndividual
type: unificationXref
DB: LIGAND
ID: c00074

unificationXref89
type: NamedIndividual
type: unificationXref
ID: 73-89-2
DB: CAS

unificationXref92
type: NamedIndividual
type: unificationXref
ID: 7732-18-5
DB: CAS

unificationXref99
type: NamedIndividual
type: unificationXref
ID: P08324
DB: SWISS-PROT