ID A0A0G3HC51_9CORY Unreviewed; 291 AA.
AC A0A0G3HC51;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AKK10966.1};
DE EC=2.1.1.10 {ECO:0000313|EMBL:AKK10966.1};
GN Name=mmuM {ECO:0000313|EMBL:AKK10966.1};
GN ORFNames=CUTER_04815 {ECO:0000313|EMBL:AKK10966.1};
OS Corynebacterium uterequi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK10966.1, ECO:0000313|Proteomes:UP000035548};
RN [1] {ECO:0000313|EMBL:AKK10966.1, ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK10966.1,
RC ECO:0000313|Proteomes:UP000035548};
RX PubMed=26227590;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Virulence Factor Genes Detected in the Complete Genome Sequence of
RT Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden
RT Mare.";
RL Genome Announc. 3:e00783-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated
RT from the uterus of a maiden mare.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505-2};
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DR EMBL; CP011546; AKK10966.1; -; Genomic_DNA.
DR RefSeq; WP_047259454.1; NZ_CP011546.1.
DR AlphaFoldDB; A0A0G3HC51; -.
DR STRING; 1072256.CUTER_04815; -.
DR KEGG; cut:CUTER_04815; -.
DR PATRIC; fig|1072256.5.peg.954; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000035548; 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|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000035548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW ProRule:PRU00333}.
FT DOMAIN 2..291
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 291 AA; 30390 MW; 4FE1874B7935E27E CRC64;
MSSFLQALAD GTPITLDGGL GTHLAARGND VTGQLWSAAI LRSNPDEVRA AHADFFAAGA
DVATTCSYQV TFDAVGEEAE ELLRRSVALA AQARTRPGQW IAASIGPYGA GPGAGTEYDG
AYGLSVAELA AWHRRRIEVL SDTEADVLWA ETVPSILEVQ ALVAELGRVP KPAVLSVTVD
SAGMRDGTSL TDLAEVVSTA SNLVAVGVNC SSAEDALAAV RQLDRVLDLP LAAYPNSGEV
WDHEARSWHR ADDDARGLLE CAGELRSAGV RLLGGCCRVT PREIAVLAGQ S
//
