9HGQ | pdb_00009hgq

Crystal Structure of the Coxiella burnetii 2-methylisocitrate lyase Bound to Substrate 2-MIC

External Resource: Annotation


Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF13714Phosphoenolpyruvate phosphomutase (PEP_mutase)Phosphoenolpyruvate phosphomutaseThis domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterised as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-P ...This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterised as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr) [1]. This enzyme has a TIM barrel fold.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
2-methylisocitrate lyase -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B
IPR015813Pyruvate/Phosphoenolpyruvate kinase-like domain superfamilyHomologous Superfamily
A, B
IPR018523Isocitrate lyase/phosphorylmutase, conserved siteConserved Site
A, B
IPR0126952-methylisocitrate lyaseFamily
A, B
IPR039556ICL/PEPM domainDomain
A, B
IPR040442Pyruvate kinase-like domain superfamilyHomologous Superfamily