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Details on Person UniProt:Q99707-2 MTR
| Class:Id | ReferenceIsoform:8968867 |
|---|---|
| _chainChangeLog | chain:1-1265 added on Fri February 17 2017 |
| _displayName | UniProt:Q99707-2 MTR |
| _timestamp | 2024-11-03 20:10:46 |
| chain | chain:1-1265 |
| checksum | B04C26BCBE9A57C2 |
| comment | FUNCTION Catalyzes the transfer of a methyl group from methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol (PubMed:16769880, PubMed:17288554, PubMed:27771510). MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate (PubMed:16769880, PubMed:17288554, PubMed:27771510). The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (PubMed:16769880, PubMed:27771510).CATALYTIC ACTIVITY (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionineCOFACTOR Binds 1 zinc ion per subunit.PATHWAY Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.SUBUNIT Monomer (PubMed:17288554). Dimer (PubMed:17288554). Forms a multiprotein complex with MMACHC, MMADHC and MTRR (PubMed:16769880, PubMed:17288554, PubMed:27771510).INTERACTION Widely expressed. Expressed at the highest levels in pancreas, heart, brain, skeletal muscle and placenta (PubMed:8968735, PubMed:8968737). Expressed at lower levels in lung, liver and kidney (PubMed:8968735, PubMed:8968737).DOMAIN Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin (By similarity).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE Disease susceptibility is associated with variants affecting the gene represented in this entry.SIMILARITY Belongs to the vitamin-B12 dependent methionine synthase family.ONLINE INFORMATION 5-methyltetrahydrofolate-homocysteine methyltransferase entry |
| created | [InstanceEdit:8964659] Weiser, JD |
| description | recommendedName: fullName evidence="21"Methionine synthase shortName: MS ecNumber evidence="11 12"2.1.1.13 alternativeName: 5-methyltetrahydrofolate--homocysteine methyltransferase alternativeName: Cobalamin-dependent methionine synthase alternativeName: Vitamin-B12 dependent methionine synthase |
| geneName | MTR |
| identifier | Q99707 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Amino-acid biosynthesis Cobalamin Cobalt Cytoplasm Disease variant Metal-binding Methionine biosynthesis Methyltransferase Phosphoprotein Proteomics identification Reference proteome Repeat S-adenosyl-L-methionine Transferase Zinc |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | MTR |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8962323] ENSEMBL:ENSG00000116984 MTR [Homo sapiens] |
| secondaryIdentifier | METH_HUMAN A1L4N8 A9Z1W4 B7ZLW7 B9EGF7 Q99713 Q99723 |
| sequenceLength | 1265 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | Q99707-2 |
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No pathways have been reviewed or authored by UniProt:Q99707-2 MTR (8968867)
