ID   A6I4V3_RAT              Unreviewed;       407 AA.
AC   A6I4V3;
DT   28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 1.
DT   24-JAN-2024, entry version 4.
DE   RecName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000256|ARBA:ARBA00040913};
DE            EC=2.1.1.5 {ECO:0000256|ARBA:ARBA00039115};
GN   ORFNames=rCG_44400 {ECO:0000313|EMBL:EDM10062.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:EDM10062.1};
RN   [1] {ECO:0000313|EMBL:EDM10062.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDM10062.1};
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [2] {ECO:0000313|EMBL:EDM10062.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDM10062.1};
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA   Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA   Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-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. {ECO:0000256|ARBA:ARBA00037521}.
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         Evidence={ECO:0000256|ARBA:ARBA00036009};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22337;
CC         Evidence={ECO:0000256|ARBA:ARBA00036009};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037505,
CC         ECO:0000256|PIRSR:PIRSR037505-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505,
CC       ECO:0000256|PIRSR:PIRSR037505-2};
CC   -!- PATHWAY: Amine and polyamine degradation; betaine degradation;
CC       sarcosine from betaine: step 1/2. {ECO:0000256|ARBA:ARBA00037879}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (BhmT route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005137, ECO:0000256|PIRNR:PIRNR037505}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|PIRNR:PIRNR037505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH473955; EDM10062.1; -; Genomic_DNA.
DR   Proteomes; UP000234681; Chromosome 2.
DR   GO; GO:0008172; F:S-methyltransferase activity; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   PANTHER; PTHR46120; BETAINE--HOMOCYSTEINE S-METHYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR46120:SF2; BETAINE--HOMOCYSTEINE S-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037505,
KW   ECO:0000256|PIRSR:PIRSR037505-2};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037505}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037505};
KW   Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}.
FT   DOMAIN          11..314
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   407 AA;  44993 MW;  983F71645A69547F CRC64;
     MAPIAGKKAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH
     REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG
     GVSQTPSYLS CKSETEVKKI FHQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKTSGKP
     IAATMCIGPE GDLHGVSPGE CAVRLVKAGA AIVGVNCHFD PSTSLQTIKL MKEGLEAARL
     KAYLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC
     GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWQNLRIASG
     RPYNPSMSKP DAWGVTKGAA ELMQQKEATT EQQLRALFEK QKFKSAQ
//