Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BMM_CoA_mutasee5cjtB3 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: MM_CoA_mutaseECOD (1.6)
BArgKe5cjtB2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: ArgKECOD (1.6)
BB12-bindinge5cjtB1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: CheY-likeF: B12-bindingECOD (1.6)
AMM_CoA_mutasee5cjtA2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: MM_CoA_mutaseECOD (1.6)
AArgKe5cjtA1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: ArgKECOD (1.6)
AB12-bindinge5cjtA3 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: CheY-likeF: B12-bindingECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF03308Methylmalonyl Co-A mutase-associated GTPase MeaB (MeaB)Methylmalonyl Co-A mutase-associated GTPase MeaBFamily members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated ...Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria [1].
Domain
A, B
PF02310B12 binding domain (B12-binding)B12 binding domainThis domain binds to B12 (adenosylcobamide)[1-3], it is found in several enzymes, such as glutamate mutase Swiss:Q05488, methionine synthase Swiss:Q99707 and methylmalonyl-CoA mutase Swiss:P22033. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, ...This domain binds to B12 (adenosylcobamide)[1-3], it is found in several enzymes, such as glutamate mutase Swiss:Q05488, methionine synthase Swiss:Q99707 and methylmalonyl-CoA mutase Swiss:P22033. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding [2].
Domain
A, B
PF01642Methylmalonyl-CoA mutase (MM_CoA_mutase)Methylmalonyl-CoA mutase- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
Isobutyryl-CoA mutase fused -