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Database: UniProt
Entry: I3XWH8_SULBS
LinkDB: I3XWH8_SULBS
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ID   I3XWH8_SULBS            Unreviewed;       311 AA.
AC   I3XWH8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:AFL68302.1};
DE            EC=2.1.1.10 {ECO:0000313|EMBL:AFL68302.1};
GN   OrderedLocusNames=Sulba_1003 {ECO:0000313|EMBL:AFL68302.1};
OS   Sulfurospirillum barnesii (strain ATCC 700032 / DSM 10660 / SES-3).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurospirillaceae; Sulfurospirillum.
OX   NCBI_TaxID=760154 {ECO:0000313|EMBL:AFL68302.1, ECO:0000313|Proteomes:UP000006176};
RN   [1] {ECO:0000313|EMBL:AFL68302.1, ECO:0000313|Proteomes:UP000006176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700032 / DSM 10660 / SES-3
RC   {ECO:0000313|Proteomes:UP000006176};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Stolz J., Arkin A.,
RA   Dehal P., Oremland R., Saltikov C., Basu P., Hollibaugh J., Newman D.,
RA   Stolyar S., Hazen T., Woyke T.;
RT   "Complete sequence of Sulfurospirillum barnesii SES-3.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
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DR   EMBL; CP003333; AFL68302.1; -; Genomic_DNA.
DR   RefSeq; WP_014769181.1; NC_018002.1.
DR   AlphaFoldDB; I3XWH8; -.
DR   STRING; 760154.Sulba_1003; -.
DR   KEGG; sba:Sulba_1003; -.
DR   PATRIC; fig|760154.4.peg.1002; -.
DR   eggNOG; COG2040; Bacteria.
DR   HOGENOM; CLU_004914_3_2_7; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000006176; Chromosome.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
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; 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; PTHR46015:SF1; ZGC:171603 PROTEIN; 1.
DR   PANTHER; PTHR46015; ZGC:172121; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 2.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          2..309
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   311 AA;  34120 MW;  02E1576EF36B0D1A CRC64;
     MNPLTPFLEA QKVFILDGAF GTELERKGYD INDSLWSAKF LMEKPEAIAE VHLDYLNAGS
     DCITTASYQA SFEGFMKRGM SEAEAKALIV SSVKIAQKVR DDFWSDTKNH VKRLKPLVAA
     SIGPYGAYLA DGSEFRGNYG LSMEALMNFH RKRLLTLIEA KPDLLACETI PCLVEAKALC
     ALLEGYPAVS AWVSFSAKDG EHINSGEKVR ECAQFLESQK QIVAIGINCT APQFIESLID
     EIKAVSSKPI IVYPNGGSSY NALTKTWDGL SKNASYGKMA YGWYQKGARL IGGCCQTTPE
     DIAQIAVWVR A
//
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