ID   BHMT1_XENTR             Reviewed;         403 AA.
AC   Q5M8Z0; Q5FWR7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Betaine--homocysteine S-methyltransferase 1;
DE            EC=2.1.1.5;
GN   Name=bhmt;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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}.
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DR   EMBL; BC087774; AAH87774.1; -; mRNA.
DR   EMBL; BC089235; AAH89235.1; -; mRNA.
DR   RefSeq; NP_001011217.1; NM_001011217.1.
DR   AlphaFoldDB; Q5M8Z0; -.
DR   SMR; Q5M8Z0; -.
DR   STRING; 8364.ENSXETP00000059123; -.
DR   PaxDb; Q5M8Z0; -.
DR   DNASU; 496651; -.
DR   Ensembl; ENSXETT00000001133; ENSXETP00000001133; ENSXETG00000000523.
DR   GeneID; 496651; -.
DR   KEGG; xtr:496651; -.
DR   CTD; 635; -.
DR   Xenbase; XB-GENE-1008382; bhmt.
DR   eggNOG; KOG1579; Eukaryota.
DR   HOGENOM; CLU_047457_0_0_1; -.
DR   InParanoid; Q5M8Z0; -.
DR   OrthoDB; 731388at2759; -.
DR   PhylomeDB; Q5M8Z0; -.
DR   Reactome; R-XTR-1614635; Sulfur amino acid metabolism.
DR   Reactome; R-XTR-6798163; Choline catabolism.
DR   UniPathway; UPA00051; UER00083.
DR   UniPathway; UPA00291; UER00432.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000523; Expressed in mesonephros and 18 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central.
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:0071267; P:L-methionine salvage; IBA:GO_Central.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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_0000273223"
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;  44154 MW;  079A8C12A4A73CDB CRC64;
     MAPTGAKKGL LERLDAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF
     LRAGANVMQT FTFYASDDKL ENRGNYVAKK ISGQKVNEAA CDIAREVANE GDALVAGGVS
     QTPSYLSCKS EVEVKGIFRK QLDVFIKKNV DFLIAEYFEH VEEAVWAVEV LKESGKPVAA
     TLCIGPQGDL NGVTPGECAV RLAKAGASVV GVNCHFDPMT CIATVKLMKE GLVAAKVKAH
     LMTQPLAYHT PDCGKQGFID LPEFPFALEP RIVTRWDIHK YAREAYNLGV RYIGGCCGFE
     PYHTRAIAEE LAPERGFLPP GSEKHGSWGS GLEMHTKPWV RARARRDYWE KLPPASGRPC
     CPSMSKPDAW GVTKGDADLM QQKEATTEQQ LIDLFAKQCI KSN