ID   BHMT1_XENLA             Reviewed;         403 AA.
AC   Q5XGM3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Betaine--homocysteine S-methyltransferase 1;
DE            EC=2.1.1.5;
GN   Name=bhmt;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of homocysteine metabolism.
CC       Converts betaine and homocysteine to dimethylglycine and methionine,
CC       respectively. This reaction is also required for the irreversible
CC       oxidation of choline (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine betaine + L-homocysteine = L-methionine + N,N-
CC         dimethylglycine; Xref=Rhea:RHEA:22336, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58251; EC=2.1.1.5;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine degradation; betaine degradation;
CC       sarcosine from betaine: step 1/2.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (BhmT route): step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC084414; AAH84414.1; -; mRNA.
DR   RefSeq; NP_001088416.1; NM_001094947.1.
DR   AlphaFoldDB; Q5XGM3; -.
DR   SMR; Q5XGM3; -.
DR   MaxQB; Q5XGM3; -.
DR   DNASU; 495275; -.
DR   GeneID; 495275; -.
DR   KEGG; xla:495275; -.
DR   CTD; 495275; -.
DR   Xenbase; XB-GENE-1008388; bhmt.L.
DR   OrthoDB; 731388at2759; -.
DR   UniPathway; UPA00051; UER00083.
DR   UniPathway; UPA00291; UER00432.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 495275; Expressed in pancreas and 17 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.330; -; 1.
DR   InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Methyltransferase; Reference proteome;
KW   Transferase; Zinc.
FT   CHAIN           1..403
FT                   /note="Betaine--homocysteine S-methyltransferase 1"
FT                   /id="PRO_0000273222"
FT   DOMAIN          8..311
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   403 AA;  44181 MW;  D7FAFA7DD70F3782 CRC64;
     MAPVGAKKGL LERLDAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF
     LRAGANVMQT FTFYASDDKL ENRGNYVAEK ISGQKVNEVA CDIAREVANE GDALVAGGVS
     QTPSYLSCKS EVEVKGIFRK QLDVFIKKNV DFLIAEYFEH VEEAVWAVEV LKESGKPVAA
     TLCIGPEGDL NGVSPGECAV RLAKAGASVV GVNCHFDPMT CVATVKLMKE GLVAAKVKAH
     LMTQPLAYHT PDCGKQGFID LPEFPFALEP RIVTRWDIHK YARAAYDLGV RYIGGCCGFE
     PYHTRAIAEE LAPERGFLPK GSEKHGSWGS GLEMHTKPWV RARARRDYWE KLPPASGRPY
     CPSMSKPDEW GVTKGDADLM QQKEATTEQQ LKDLIAKQGI KSN