ID   HMT_BACSU               Reviewed;         315 AA.
AC   O31463; Q7DL43;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Homocysteine S-methyltransferase YbgG;
DE            EC=2.1.1.10;
DE   AltName: Full=S-methylmethionine:homocysteine methyltransferase;
GN   Name=ybgG; OrderedLocusNames=BSU02410;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9455481; DOI=10.1093/dnares/4.5.329;
RA   Haga K., Liu H., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of a 45-kb segment in the 19 degrees-23 degrees region
RT   of the Bacillus subtilis chromosome containing glpT and mpr loci.";
RL   DNA Res. 4:329-333(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=11267663; DOI=10.1016/s0167-4781(01)00182-8;
RA   Yazgan A., Oezcengiz G., Marahiel M.A.;
RT   "Tn10 insertional mutations of Bacillus subtilis that block the
RT   biosynthesis of bacilysin.";
RL   Biochim. Biophys. Acta 1518:87-94(2001).
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;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00333};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show reduced bacilysin
CC       biosynthetic activity. {ECO:0000269|PubMed:11267663}.
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DR   EMBL; AB006424; BAA33139.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12035.1; -; Genomic_DNA.
DR   PIR; B69751; B69751.
DR   RefSeq; NP_388123.1; NC_000964.3.
DR   RefSeq; WP_003246467.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; O31463; -.
DR   SMR; O31463; -.
DR   STRING; 224308.BSU02410; -.
DR   PaxDb; O31463; -.
DR   PRIDE; O31463; -.
DR   DNASU; 938412; -.
DR   EnsemblBacteria; CAB12035; CAB12035; BSU_02410.
DR   GeneID; 938412; -.
DR   KEGG; bsu:BSU02410; -.
DR   PATRIC; fig|224308.179.peg.247; -.
DR   eggNOG; COG2040; Bacteria.
DR   InParanoid; O31463; -.
DR   OMA; HRPRMKA; -.
DR   PhylomeDB; O31463; -.
DR   BioCyc; BSUB:BSU02410-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central.
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   4: Predicted;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN           1..315
FT                   /note="Homocysteine S-methyltransferase YbgG"
FT                   /id="PRO_0000379124"
FT   DOMAIN          2..309
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         229
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"
SQ   SEQUENCE   315 AA;  34736 MW;  01B6F2DD00180D67 CRC64;
     MNPIQHILDT YPLIVLDGAM ATELERKGCN LNDSLWSAKI LMEEPELIKQ VHTDYFAAGA
     DCAITASYQS TFEGFAARGL SEAEARRLIE LSVSIAAEAR DEFWSLEENR LNRPKPIIAA
     SIGPYGAYLA DGSEYRGNYA ISEDELIEFH RPRMKALIEA GADVLACETI PCLTEAKAIV
     RLLKEFPETY AWISFSAKDG LHISDGTPAA DCASWLDEHR QIAALGINCT PLQHIPSLIE
     ELKKNTSKPI IVYPNSGEQY DPETKTWNGA ACAESYGASA RTWHEKGARL IGGCCRTKPE
     NIQEIAAWAR SLKTT