Methionine synthase

MTR
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2O2K, 4CCZ
Identifiers
Aliases	MTR, HMAG, MS, cblG, 5-methyltetrahydrofolate-homocysteine methyltransferase
External IDs	OMIM: 156570 MGI: 894292 HomoloGene: 37280 GeneCards: MTR
EC number	2.1.1.13
Gene ontology Molecular function • methyltransferase activity • S-adenosylmethionine-homocysteine S-methyltransferase activity • protein binding • methionine synthase activity • zinc ion binding • cobalamin binding • metal ion binding • transferase activity Cellular component • intracellular • cytoplasm • cytosol Biological process • sulfur amino acid metabolic process • nervous system development • methylation • pteridine-containing compound metabolic process • methionine biosynthetic process • response to axon injury • cellular amino acid biosynthetic process • cobalamin metabolic process • cellular response to nitric oxide • axon regeneration • cellular metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4548	238505
Ensembl	ENSG00000116984	ENSMUSG00000021311
UniProt	Q99707	A6H5Y3
RefSeq (mRNA)	NM_000254 NM_001291939 NM_001291940	NM_001081128
RefSeq (protein)	NP_000245 NP_001278868 NP_001278869	NP_001074597.1 NP_001074597
Location (UCSC)	Chr 1: 236.8 – 236.9 Mb	Chr 13: 12.19 – 12.26 Mb
PubMed search

2O2K, 4CCZ

4548

238505

ENSG00000116984

ENSMUSG00000021311

Q99707

A6H5Y3

NM_000254
NM_001291939
NM_001291940

NM_001081128

NP_000245
NP_001278868
NP_001278869

NP_001074597.1
NP_001074597

Methionine synthase also known as MS, MeSe, MetH is responsible for the regeneration of methionine from homocysteine. In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle. In animals this enzyme requires Vitamin B12 (cobalamin) as a cofactor, whereas the form found in plants is cobalamin-independent. Microorganisms express both cobalamin-dependent and cobalamin-independent forms.

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