2NX9

Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e2nx9A1	A: alpha arrays	X: RuvA-C	H: post-HMGL domain-like (From Topology)	T: post-HMGL domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF02436	e2nx9A3	A: alpha arrays	X: RuvA-C	H: post-HMGL domain-like (From Topology)	T: post-HMGL domain-like	F: PF02436	ECOD (1.6)
A	PF00682	e2nx9A2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00682	ECOD (1.6)
B	F_UNCLASSIFIED	e2nx9B2	A: alpha arrays	X: RuvA-C	H: post-HMGL domain-like (From Topology)	T: post-HMGL domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF02436	e2nx9B3	A: alpha arrays	X: RuvA-C	H: post-HMGL domain-like (From Topology)	T: post-HMGL domain-like	F: PF02436	ECOD (1.6)
B	PF00682	e2nx9B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00682	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00682	HMGL-like (HMGL-like)	HMGL-like	This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.	Domain
A, B	PF02436	Conserved carboxylase domain (PYC_OADA)	Conserved carboxylase domain	This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (Pfam:PF00682) and often close to the bio ...	This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (Pfam:PF00682) and often close to the biotin_lipoyl domain (Pfam:PF00364) of biotin requiring enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Oxaloacetate decarboxylase 2, subunit alpha	carboxyl- or carbamoyltransferase activity methylmalonyl-CoA carboxytransferase activity transferase activity, transferring one-carbon groups transferase activity catalytic activity pyruvate carboxylase activity ligase activity, forming carbon-carbon bonds ligase activity oxaloacetate decarboxylase activity carboxy-lyase activity lyase activity carbon-carbon lyase activity cation binding ion binding carboxyl- or carbamoyltransferase activity methylmalonyl-CoA carboxytransferase activity transferase activity, transferring one-carbon groups transferase activity catalytic activity pyruvate carboxylase activity ligase activity, forming carbon-carbon bonds ligase activity oxaloacetate decarboxylase activity carboxy-lyase activity lyase activity carbon-carbon lyase activity cation binding ion binding binding metal ion binding small molecule binding	localization transport monoatomic ion transport monoatomic cation transport establishment of localization sodium ion transport metal ion transport organic substance metabolic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B	IPR005776	Oxaloacetate decarboxylase, alpha subunit	Family
A, B	IPR000891	Pyruvate carboxyltransferase	Domain
A, B	IPR003379	Carboxylase, conserved domain	Domain
A, B	IPR011053	Single hybrid motif	Homologous Superfamily
A, B	IPR001882	Biotin-binding site	Binding Site
A, B	IPR000089	Biotin/lipoyl attachment	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.