ID D5AKC8_STRGZ Unreviewed; 315 AA.
AC D5AKC8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADE32293.1};
GN OrderedLocusNames=SSGZ1_1837 {ECO:0000313|EMBL:ADE32293.1};
OS Streptococcus suis (strain GZ1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE32293.1, ECO:0000313|Proteomes:UP000002359};
RN [1] {ECO:0000313|EMBL:ADE32293.1, ECO:0000313|Proteomes:UP000002359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GZ1 {ECO:0000313|EMBL:ADE32293.1,
RC ECO:0000313|Proteomes:UP000002359};
RX PubMed=19016627; DOI=10.1086/594370;
RA Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., Zhou Z.,
RA Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT "Clinical, experimental, and genomic differences between intermediately
RT pathogenic, highly pathogenic, and epidemic Streptococcus suis.";
RL J. Infect. Dis. 199:97-107(2009).
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; CP000837; ADE32293.1; -; Genomic_DNA.
DR RefSeq; WP_012775454.1; NC_017617.1.
DR AlphaFoldDB; D5AKC8; -.
DR KEGG; ssw:SSGZ1_1837; -.
DR PATRIC; fig|423211.3.peg.1809; -.
DR HOGENOM; CLU_004914_3_2_9; -.
DR Proteomes; UP000002359; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
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};
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..314
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 233
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 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 315 AA; 34868 MW; AAC726145F5E324F CRC64;
MGRFKELLEQ KEYIILHGAL GTELEFRGHD VSGKLWSAKY LLENPQYIKD IHKDYIRAGA
DLVTTSTYQA TFEGLAEVGL SQAEAEELIR LTVDLAKEAR DEVWAELSEA EKVQRTYPLI
SGDVGPYAAY LANGAEYTGD YGNISLSELK DFHRRRIELL LEQEAELLAL ETIPNVLEAQ
ALVELLAEDF PEAEAYISFT SQDGQSISDG TSIEKIAELV NSSEQILAVG LNCTAPSLYP
AFLSQLREKT DKPFVTYPNS GEVYDGATQT WKEKADDSHS LLDNTLEWHE LGAKVVGGCC
RTRPADIADL VAGLK
//
