ID   BHMT2_PONAB             Reviewed;         363 AA.
AC   Q5RF32;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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=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; CR857329; CAH89625.1; -; mRNA.
DR   RefSeq; NP_001127177.1; NM_001133705.2.
DR   AlphaFoldDB; Q5RF32; -.
DR   SMR; Q5RF32; -.
DR   STRING; 9601.ENSPPYP00000024408; -.
DR   Ensembl; ENSPPYT00000018128; ENSPPYP00000017422; ENSPPYG00000015585.
DR   GeneID; 100174229; -.
DR   KEGG; pon:100174229; -.
DR   CTD; 23743; -.
DR   eggNOG; KOG1579; Eukaryota.
DR   GeneTree; ENSGT00390000003122; -.
DR   HOGENOM; CLU_047457_0_0_1; -.
DR   InParanoid; Q5RF32; -.
DR   UniPathway; UPA00051; UER00083.
DR   Proteomes; UP000001595; Chromosome 5.
DR   GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; -; 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; Phosphoprotein; Reference proteome;
KW   Transferase; Zinc.
FT   CHAIN           1..363
FT                   /note="S-methylmethionine--homocysteine S-methyltransferase
FT                   BHMT2"
FT                   /id="PRO_0000273226"
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"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2M3"
SQ   SEQUENCE   363 AA;  40336 MW;  D2B34B3F8EF4A103 CRC64;
     MAPAGHPGAK RGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH
     MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK
     YHKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCISP
     EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPETSLKTIE LMKEGLQRAG LKAHLMVQPL
     GFHTPDCGKE GFVDLPEYPF GLESRAATRW DIQKYAREAY NQGVRYIGGC CGFEPYHIRA
     IAEELAPERG FLPPASEKHG SWGSALDMHT KPWVRARARR EYWENLLPAS GRPFCPSLSK
     PDV