Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APYC_OADA_1ste2qf7A2 A: alpha arraysX: RuvA-CH: post-HMGL domain-like (From Topology)T: post-HMGL domain-likeF: PYC_OADA_1stECOD (1.6)
APYC_OADA_2nd_1e2qf7A7 A: alpha arraysX: RuvA-CH: post-HMGL domain-like (From Topology)T: post-HMGL domain-likeF: PYC_OADA_2nd_1ECOD (1.6)
APYC_OADA_3rde2qf7A5 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: a+b domain in pyruvate carboxylaseF: PYC_OADA_3rdECOD (1.6)
AATP-graspe2qf7A3 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: ATP-graspF: ATP-graspECOD (1.6)
ABiotin_carb_Ce2qf7A4 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: Biotin_carb_CECOD (1.6)
ABiotin_lipoyle2qf7A8 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: Single hybrid motifF: Biotin_lipoylECOD (1.6)
AHMGL-like_2e2qf7A1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: HMGL-like_2ECOD (1.6)
ABiotin_carb_Ne2qf7A6 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: PreATP-grasp domainF: Biotin_carb_NECOD (1.6)
BPYC_OADA_1ste2qf7B12 A: alpha arraysX: RuvA-CH: post-HMGL domain-like (From Topology)T: post-HMGL domain-likeF: PYC_OADA_1stECOD (1.6)
BPYC_OADA_2nd_1e2qf7B17 A: alpha arraysX: RuvA-CH: post-HMGL domain-like (From Topology)T: post-HMGL domain-likeF: PYC_OADA_2nd_1ECOD (1.6)
BPYC_OADA_3rde2qf7B14 A: a+b two layersX: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-related (From Homology)H: Methylcrotonyl-CoA carboxylase alpha-subunit BT domain-relatedT: a+b domain in pyruvate carboxylaseF: PYC_OADA_3rdECOD (1.6)
BATP-graspe2qf7B13 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: ATP-graspF: ATP-graspECOD (1.6)
BBiotin_carb_Ce2qf7B16 A: a+b complex topologyX: alpha/beta-Hammerhead/Barrel-sandwich hybridH: alpha/beta-Hammerhead/Barrel-sandwich hybridT: CO dehydrogenase molybdoprotein N-domain-likeF: Biotin_carb_CECOD (1.6)
BHMGL-like_2e2qf7B11 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: HMGL-like_2ECOD (1.6)
BBiotin_carb_Ne2qf7B15 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: PreATP-grasp domainF: Biotin_carb_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00682HMGL-like (HMGL-like)HMGL-likeThis family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.Domain
A, B
PF00364Biotin-requiring enzyme (Biotin_lipoyl)Biotin-requiring enzymeThis family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognise the Glycine cleavage system H proteins.Domain
A, B
PF02786Carbamoyl-phosphate synthase L chain, ATP binding domain (CPSase_L_D2)Carbamoyl-phosphate synthase L chain, ATP binding domainCarbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines [2]. The c ...Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines [2]. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. See Pfam:PF00988. The small chain has a GATase domain in the carboxyl terminus. See Pfam:PF00117. The ATP binding domain (this one) has an ATP-grasp fold.
Domain
A, B
PF02785Biotin carboxylase C-terminal domain (Biotin_carb_C)Biotin carboxylase C-terminal domainBiotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference [1] are i ...Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference [1] are in this C-terminal domain.
Domain
A, B
PF00289Biotin carboxylase, N-terminal domain (Biotin_carb_N)Biotin carboxylase, N-terminal domainThis domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes [1,3], and propionyl-CoA carboxylase A chain [2].Domain
A, B
PF02436Conserved carboxylase domain (PYC_OADA)Conserved carboxylase domainThis 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

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
Pyruvate carboxylase protein

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
pyruvate carboxylase  M-CSA #223

Pyruvate carboxylase, isolated from Rhizobium etli, is a biotin-dependent enzyme. It catalyses the carboxylation of pyruvate to oxaloacetate using bicarbonate and coupled to the hydrolysis of ATP to ADP and phosphate. This reaction occurs in two major steps: the carboxylation of biotin by ATP and bicarbonate in the biotin carboxylase (BC) domain, and the carboxylation of pyruvate in the carboxyltransferase (CT) domain. The biotin is bound to the biotin carboxyl carrier protein (BCCP) domain, which moves between the BC domain of one subunit and the CT domain of a neighbouring subunit.

Defined by 11 residues: GLU:A-294 [auth A-283]GLU:A-308 [auth A-297]ASN:A-310 [auth A-299]GLU:A-316 [auth A-305]ARG:A-364 [auth A-353]ASP:A-560 [auth A-549]ASP:A-666 [auth A-655]LYS:A-729 [auth A-718]HIS:A-758 [auth A-747]HIS:A-760 [auth A-749]THR:A-893 [auth A-882]
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Explore in 3DM-CSA Motif Definition
Up to 10 residues are supported for Structure Motif searching, this motif has 11 residues.
EC: 6.4.1.1 (PDB Primary Data)