ID C3M8I7_SINFN Unreviewed; 322 AA.
AC C3M8I7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACP24533.1};
DE EC=2.1.1.10 {ECO:0000313|EMBL:ACP24533.1};
GN OrderedLocusNames=NGR_c07400 {ECO:0000313|EMBL:ACP24533.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24533.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP24533.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
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DR EMBL; CP001389; ACP24533.1; -; Genomic_DNA.
DR RefSeq; WP_012707318.1; NC_012587.1.
DR RefSeq; YP_002825286.1; NC_012587.1.
DR AlphaFoldDB; C3M8I7; -.
DR STRING; 394.NGR_c07400; -.
DR KEGG; rhi:NGR_c07400; -.
DR PATRIC; fig|394.7.peg.3556; -.
DR eggNOG; COG2040; Bacteria.
DR HOGENOM; CLU_062282_0_0_5; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000001054; 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; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11103; SLR1189 PROTEIN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 8..314
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 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 322 AA; 35489 MW; F184C68C9F1285AC CRC64;
MQHEFAKYRH DLPLLQGGTF LSDGGMETAL IFQEGVELPH FASFVLLSSM EGRRQLLHYY
TSYLEIARCR DTGFVLDTAT WRANADWGEK LGYDAEDLDQ VNRDAVYLLT ELRAQYERPQ
VPIVFNGVIG PRGDGYKAGM MNAAEAEDYH AAQVAAFADS EADMVSAVTM TNVDEAIGVA
RAARTHGMPC AISFTVETDG RLVTGRSLQE AVETVDAETE AYPHYYMVNC AHPSHFESSL
DQDQAWVRRI GGIRANASTK SHAELDESET LDIGDINDLA RRYRSLTGRL PHLRVLGGCC
GTDHRHIAAI CEACLPPVAL SA
//
