UniProt:Q99707 MTR

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:27771510, PubMed:17288554). 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:27771510, PubMed:17288554). 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:17288554, PubMed:16769880, PubMed:27771510).INTERACTION Widely expressed. Expressed at the highest levels in pancreas, heart, brain, skeletal muscle and placenta (PubMed:8968737, PubMed:8968735). Expressed at lower levels in lung, liver and kidney (PubMed:8968737, PubMed:8968735).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
crossReference
databaseName UniProt
dbId 59167
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
displayName UniProt:Q99707 MTR
geneName
  • MTR
identifier Q99707
isSequenceChanged false
keyword
  • 3D-structure
  • Alternative splicing
  • Amino-acid biosynthesis
  • Cobalamin
  • Cobalt
  • Cytoplasm
  • Disease variant
  • Metal-binding
  • Methionine biosynthesis
  • Methyltransferase
  • Phosphoprotein
  • Reference proteome
  • Repeat
  • S-adenosyl-L-methionine
  • Transferase
  • Zinc
modified [InstanceEdit:12187927] Wright, Adam, 2024-03-12
name
  • MTR
otherIdentifier
  • 11739412_a_at
  • 11739413_at
  • 11751961_s_at
  • 11751974_a_at
  • 11756051_a_at
  • 16679094
  • 203774_PM_at
  • 203774_at
  • 226969_PM_at
  • 226969_at
  • 2387007
  • 2387008
  • 2387009
  • 2387014
  • 2387015
  • 2387016
  • 2387018
  • 2387019
  • 2387020
  • 2387021
  • 2387029
  • 2387030
  • 2387031
  • 2387032
  • 2387035
  • 2387037
  • 2387038
  • 2387039
  • 2387040
  • 2387044
  • 2387045
  • 2387046
  • 2387048
  • 2387049
  • 2387050
  • 2387051
  • 2387054
  • 2387055
  • 2387057
  • 2387060
  • 2387061
  • 2387064
  • 2387067
  • 2387069
  • 2387072
  • 2387073
  • 2387074
  • 2387075
  • 2387076
  • 2387081
  • 2387082
  • 2387083
  • 2387085
  • 38383_at
  • 44615_at
  • 4548
  • 75377_at
  • 7910752
  • A_14_P132244
  • A_23_P200930
  • A_23_P200936
  • A_24_P67806
  • A_33_P3389917
  • GE80903
  • GO:0003824
  • GO:0005515
  • GO:0005737
  • GO:0005829
  • GO:0006520
  • GO:0006575
  • GO:0006766
  • GO:0006790
  • GO:0007399
  • GO:0008168
  • GO:0008172
  • GO:0008270
  • GO:0008652
  • GO:0008705
  • GO:0009086
  • GO:0009235
  • GO:0016740
  • GO:0030154
  • GO:0031103
  • GO:0031419
  • GO:0032259
  • GO:0042558
  • GO:0044237
  • GO:0046653
  • GO:0046872
  • GO:0048678
  • GO:0048856
  • GO:0050667
  • GO:0071732
  • HMNXSV003018013
  • HMNXSV003030237
  • Hs.33264.0.A1_3p_at
  • ILMN_1670801
  • ILMN_1815141
  • PH_hs_0040560
  • TC01001956.hg
  • TC01005133.hg
  • U73338_at
  • g4557764_3p_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • METH_HUMAN
  • A1L4N8
  • A9Z1W4
  • B7ZLW7
  • B9EGF7
  • Q99713
  • Q99723
sequenceLength 1265
species [Species:48887] Homo sapiens
url https://purl.uniprot.org/uniprot/Q99707
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