Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AATP-graspe2c00A2 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_Ce2c00A3 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_carb_Ne2c00A1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: PreATP-grasp domainF: Biotin_carb_NECOD (1.6)
BATP-graspe2c00B1 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_Ce2c00B2 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)
BBiotin_carb_Ne2c00B3 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: PreATP-grasp domainF: Biotin_carb_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.20 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
A3.30.470.20 Alpha Beta 2-Layer Sandwich D-amino Acid Aminotransferase Chain A, domain 1CATH (4.3.0)
A3.30.1490.20 Alpha Beta 2-Layer Sandwich Dna Ligase domain 1CATH (4.3.0)
B3.40.50.20 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
B3.30.470.20 Alpha Beta 2-Layer Sandwich D-amino Acid Aminotransferase Chain A, domain 1CATH (4.3.0)
B3.30.1490.20 Alpha Beta 2-Layer Sandwich Dna Ligase domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
BIOTIN CARBOXYLASE -