ID A6I4V3_RAT Unreviewed; 407 AA. AC A6I4V3; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 27-NOV-2024, entry version 9. 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=L-homocysteine + glycine betaine = N,N-dimethylglycine + L- CC methionine; 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}. 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; CH473955; EDM10062.1; -; Genomic_DNA. DR Proteomes; UP000234681; Chromosome 2. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 FunFam; 3.20.20.330:FF:000003; Betaine--homocysteine S-methyltransferase 1; 1. DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR051524; 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 //