Annotations: 4XC6

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	MM_CoA_mutase	e4xc6B3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: MM_CoA_mutase	ECOD (1.6)
B	ArgK	e4xc6B1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: ArgK	ECOD (1.6)
B	B12-binding	e4xc6B2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: CheY-like	F: B12-binding	ECOD (1.6)
A	MM_CoA_mutase	e4xc6A3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: MM_CoA_mutase	ECOD (1.6)
A	ArgK	e4xc6A2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: ArgK	ECOD (1.6)
A	B12-binding	e4xc6A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: CheY-like	F: B12-binding	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03308	Methylmalonyl Co-A mutase-associated GTPase MeaB (MeaB)	Methylmalonyl Co-A mutase-associated GTPase MeaB	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 ...	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	PF02310	B12 binding domain (B12-binding)	B12 binding domain	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, ...	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	PF01642	Methylmalonyl-CoA mutase (MM_CoA_mutase)	Methylmalonyl-CoA mutase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Isobutyryl-CoA mutase fused	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding pivalyl-CoA mutase activity isomerase activity catalytic activity intramolecular transferase activity methylmalonyl-CoA mutase activity vitamin binding cobalamin binding organic cyclic compound binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding pivalyl-CoA mutase activity isomerase activity catalytic activity intramolecular transferase activity methylmalonyl-CoA mutase activity vitamin binding cobalamin binding organic cyclic compound binding tetrapyrrole binding heterocyclic compound binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding anion binding carbohydrate derivative binding ribonucleotide binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides isobutyryl-CoA mutase activity	nucleoside phosphate metabolic process primary metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process sulfur compound metabolic process small molecule metabolic process amide metabolic process thioester metabolic process nucleoside phosphate metabolic process primary metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process sulfur compound metabolic process small molecule metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR053439	Isobutyryl-CoA Mutase/GTPase Domain-Containing Protein	Family
A, B	IPR006098	Methylmalonyl-CoA mutase, alpha chain, catalytic	Domain
A, B	IPR033669	Fused isobutyryl-CoA mutase	Family
A, B	IPR006158	Cobalamin (vitamin B12)-binding domain	Domain
A, B	IPR006099	Methylmalonyl-CoA mutase, alpha/beta chain, catalytic	Domain
A, B	IPR036724	Cobalamin-binding domain superfamily	Homologous Superfamily
A, B	IPR052040	GTPase and isobutyryl-CoA mutase domain-containing protein	Family
A, B	IPR006159	Methylmalonyl-CoA mutase, C-terminal	Domain
A, B	IPR016176	Cobalamin (vitamin B12)-dependent enzyme, catalytic	Homologous Superfamily
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

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 R01GM157729.