ID   BHMT2_RAT               Reviewed;         363 AA.
AC   Q68FT5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2;
DE            Short=SMM-hcy methyltransferase;
DE            EC=2.1.1.10;
DE   AltName: Full=Betaine--homocysteine S-methyltransferase 2;
GN   Name=Bhmt2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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=L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-
CC         methionine; Xref=Rhea:RHEA:26337, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58252; EC=2.1.1.10;
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: 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}.
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DR   EMBL; BC079366; AAH79366.1; -; mRNA.
DR   RefSeq; NP_001014278.2; NM_001014256.2.
DR   AlphaFoldDB; Q68FT5; -.
DR   SMR; Q68FT5; -.
DR   STRING; 10116.ENSRNOP00000058419; -.
DR   iPTMnet; Q68FT5; -.
DR   PhosphoSitePlus; Q68FT5; -.
DR   PaxDb; Q68FT5; -.
DR   PRIDE; Q68FT5; -.
DR   GeneID; 365972; -.
DR   KEGG; rno:365972; -.
DR   UCSC; RGD:1359418; rat.
DR   CTD; 23743; -.
DR   RGD; 1359418; Bhmt2.
DR   eggNOG; KOG1579; Eukaryota.
DR   InParanoid; Q68FT5; -.
DR   OrthoDB; 731388at2759; -.
DR   PhylomeDB; Q68FT5; -.
DR   Reactome; R-RNO-1614635; Sulfur amino acid metabolism.
DR   UniPathway; UPA00051; UER00083.
DR   PRO; PR:Q68FT5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR   GO; GO:0071267; P:L-methionine salvage; ISO:RGD.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:RGD.
DR   GO; GO:0033477; P:S-methylmethionine metabolic process; ISO:RGD.
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   Metal-binding; Methyltransferase; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..363
FT                   /note="S-methylmethionine--homocysteine S-methyltransferase
FT                   BHMT2"
FT                   /id="PRO_0000273227"
FT   DOMAIN          11..305
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   363 AA;  39929 MW;  403AAC188B979BFE CRC64;
     MAPAGGPRVK KVILERLDSG EVVVGDGGFL FTLEKRGFVK AGLWTPEAVV EYPSAVRQLH
     TEFLRAGADV LQTFTFSAAE DRMESKWEAV NAAACDLAQE VADGGAALVA GGICQTSLYK
     YHKDETRIKN IFRLQLGVFA RKNVDFLIAE YFEHVEEAVW AVEVLREVGA PVAVTMCIGP
     EGDMHGVTPG ECAVRLSRAG ANIIGVNCRF GPWTSLQTMK LMKEGLRDAG LQAHLMVQCL
     GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA
     IAEELAPERG FLPPASEKHG IWGSGLDMHT KPWIRARARR EYWETLLPAS GRPFCPSLSK
     PDA