ID A0A0D5M1R8_9GAMM Unreviewed; 319 AA.
AC A0A0D5M1R8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AJY50047.1};
DE EC=2.1.1.10 {ECO:0000313|EMBL:AJY50047.1};
GN ORFNames=KO116_01562 {ECO:0000313|EMBL:AJY50047.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY50047.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY50047.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY50047.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
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DR EMBL; CP011052; AJY50047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D5M1R8; -.
DR STRING; 1504981.KO116_01562; -.
DR KEGG; hak:KO116_01562; -.
DR eggNOG; COG2040; Bacteria.
DR HOGENOM; CLU_004914_3_2_6; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
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 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 5..316
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 319 AA; 34002 MW; 0B093696651B3178 CRC64;
MNELNPIKAL LADVPFMVID GAMATELEAL GCDLNDALWS ARLLAQAPEK IRQVHQAYFE
AGADCAITAS YQATVPGFMQ AGMTAEEARA LIQLSVTLAQ QARDAVWQPG QTDRPKPLVA
ASVGPYGAYL ADGSEYRGGY DLDRAGLVEF HRERFELLLA AGADLLAAET LPSLEEALAI
TDLLAEHPGA QAWITFSAKD GQHISDGTPI EKCAAALANC PGVAAIGVNC TALTHIESLI
QAIRRQCDLP VLVYPNSGEV YDAVTKTWHP AQCDHTAADI SGLAQGVEHW LAAGVSGIGG
CCRTTPEDIH SLSEWRRSR
//
