Bhmt
entrez
81508
canonical
uniprot
O09171
canonical
ensembl
ENSRNOG00000011200
resolver
ensp
ENSRNOP00000015336
resolver
genesymbol
Bhmt
resolver
uniprot
Q6AZ06
resolver
uniprot_entry
BHMT1_RAT
resolver
uniprot_sec
Q6AZ06
resolver
amino_acid_sequence
MAPIAGKKAKRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLHREFLRAGSNVMQTFTFYASEDKLENRGNYVAEKISGQKVNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAATMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTSLQTIKLMKEGLEAARLKAYLMSHALAYHTPDCGKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQQKEATTEQQLRALFEKQKFKSAQ
uniprot
proteins
ec_number
2.1.1.5
uniprot
proteins
function
FUNCTION: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline. {ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}.
uniprot
proteins
mass_dalton
44976
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="K->A: Has no effect on tetramer assembly or catalytic efficiency."; /evidence="ECO:0000269|PubMed:28288879"; MUTAGEN 8; /note="K->A: Has no effect on tetramer assembly. Decreases the catalytic efficiency."; /evidence="ECO:0000269|PubMed:28288879"; MUTAGEN 10; /note="K->A: Has no effect on tetramer assembly. Decreases the catalytic efficiency. Alters nucleocytoplasmic distribution."; /evidence="ECO:0000269|PubMed:28288879"; MUTAGEN 11; /note="R->A: Has no effect on tetramer assembly."; /evidence="ECO:0000269|PubMed:28288879"; MUTAGEN 21; /note="E->A,K: Decreases the catalytic efficiency. Increases the affinity for L-homocysteine."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 26; /note="D->A,I: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 73; /note="T->G: Decreases the catalytic efficiency."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 74; /note="F->A: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 77; /note="Y->A: Decreases the catalytic efficiency."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 119; /note="A->G: Decreases the catalytic efficiency."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 159; /note="E->G,K: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 184; /note="T->G: Decreases the catalytic efficiency."; /evidence="ECO:0000269|PubMed:12487625"; MUTAGEN 186; /note="C->A,S: Decreases the catalytic efficiency. Increases the affinity for L-homocysteine."; /evidence="ECO:0000269|PubMed:12487625
uniprot
proteins
pathway_participation
PATHWAY: Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 1/2.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1. {ECO:0000305|PubMed:12487625}.
uniprot
proteins
pubmed
10417327
uniprot
proteins
pubmed
12487625
uniprot
proteins
pubmed
15099744
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
28288879
uniprot
proteins
pubmed
8753772
uniprot
proteins
sequence_length
407
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}. Nucleus {ECO:0000269|PubMed:28288879}. Note=Predominantly localized in the cytoplasm with a small fraction detected in the nucleus. Translocates into the nucleus upon oxidative stress. {ECO:0000269|PubMed:28288879}.
uniprot
proteins