ID   BHMT1_DANRE             Reviewed;         400 AA.
AC   Q32LQ4; Q5PSM1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Betaine--homocysteine S-methyltransferase 1;
DE            EC=2.1.1.5;
GN   Name=bhmt; ORFNames=wu:fb53h01, zgc:123027;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lapek J.D. Jr., Warren J.T. Jr.;
RT   "Molecular genetic analysis of folate metabolism in the zebrafish.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2005) 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; AY830415; AAV74219.1; -; mRNA.
DR   EMBL; BC109472; AAI09473.1; -; mRNA.
DR   RefSeq; NP_001012498.1; NM_001012480.1.
DR   AlphaFoldDB; Q32LQ4; -.
DR   SMR; Q32LQ4; -.
DR   STRING; 7955.ENSDARP00000040421; -.
DR   PaxDb; Q32LQ4; -.
DR   PRIDE; Q32LQ4; -.
DR   GeneID; 322228; -.
DR   KEGG; dre:322228; -.
DR   CTD; 635; -.
DR   ZFIN; ZDB-GENE-030131-947; bhmt.
DR   eggNOG; KOG1579; Eukaryota.
DR   InParanoid; Q32LQ4; -.
DR   OrthoDB; 731388at2759; -.
DR   PhylomeDB; Q32LQ4; -.
DR   Reactome; R-DRE-1614635; Sulfur amino acid metabolism.
DR   Reactome; R-DRE-6798163; Choline catabolism.
DR   UniPathway; UPA00051; UER00083.
DR   UniPathway; UPA00291; UER00432.
DR   PRO; PR:Q32LQ4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0055123; P:digestive system development; IMP:ZFIN.
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   GO; GO:0003323; P:type B pancreatic cell development; IMP:ZFIN.
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..400
FT                   /note="Betaine--homocysteine S-methyltransferase 1"
FT                   /id="PRO_0000273221"
FT   DOMAIN          8..309
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   CONFLICT        189
FT                   /note="H -> P (in Ref. 1; AAV74219)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="I -> T (in Ref. 1; AAV74219)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="A -> V (in Ref. 1; AAV74219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  44066 MW;  A6A3A9A824D5D26A CRC64;
     MAPVGSKRGV LERLNAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF
     LRAGSNVMQT FTFYASDDKL ENRGNKLSFT GQQINEAACD LAREVANEGD ALVAGGVSQT
     PSYLSCKSEE EVKKTFKKQL DVFIKKNVDL LIAEYFEHVE EAEWAVQVLK ATGKPVAATL
     CIGPDGDMHG VIPGECAVRL VKAGADIVGV NCHFDPLTCV KTVAMMKAAV EKAGLKAHYM
     TQPLAYHTPD CSCQGFIDLP EFPFALEPRI LTRWEMQQYA REAYKAGIRY IGGCCGFEPY
     HIRAVAEELS AERGFLPEAS QKHGLWGSGL EMHTKPWVRA RARRDYWEKL KPASGRPLCP
     SMSTPDGWGV TRGHAALMQQ KEATTAEQLR PLFQQADAKH