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Database: UniProt/TrEMBL
Entry: Q7CJG9_YERPE
LinkDB: Q7CJG9_YERPE
Original site: Q7CJG9_YERPE 
ID   Q7CJG9_YERPE            Unreviewed;       292 AA.
AC   Q7CJG9; Q74SH0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   10-MAY-2017, entry version 97.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   Name=cysM {ECO:0000313|EMBL:CAL21614.1};
GN   OrderedLocusNames=YPO3011 {ECO:0000313|EMBL:CAL21614.1};
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632 {ECO:0000313|Proteomes:UP000000815};
RN   [1] {ECO:0000313|EMBL:CAL21614.1, ECO:0000313|Proteomes:UP000000815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815};
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
RA   Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S.,
RA   Karlyshev A.V., Moule S., Oyston P.C.F., Quail M., Rutherford K.,
RA   Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
CC   -!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L-
CC       cysteine + acetate. {ECO:0000256|RuleBase:RU003985}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR605856-50,
CC         ECO:0000256|RuleBase:RU003985};
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; AL590842; CAL21614.1; -; Genomic_DNA.
DR   PIR; AC0366; AC0366.
DR   RefSeq; WP_002208508.1; NZ_LT605018.1.
DR   RefSeq; WP_002208508.1; NZ_LT605018.1.
DR   RefSeq; WP_002208508.1; NZ_LT605018.1.
DR   RefSeq; YP_002347933.1; NC_003143.1.
DR   RefSeq; YP_002347933.1; NC_003143.1.
DR   RefSeq; YP_002347933.1; NC_003143.1.
DR   STRING; 187410.y1470; -.
DR   DNASU; 1146417; -.
DR   EnsemblBacteria; AAM85041; AAM85041; y1470.
DR   EnsemblBacteria; AAS62827; AAS62827; YP_2635.
DR   GeneID; 1175833; -.
DR   KEGG; ype:YPO3011; -.
DR   KEGG; ypj:CH55_4058; -.
DR   KEGG; ypk:y1470; -.
DR   KEGG; ypl:CH46_2087; -.
DR   KEGG; ypm:YP_2635; -.
DR   KEGG; ypv:BZ15_515; -.
DR   KEGG; ypw:CH59_3057; -.
DR   eggNOG; ENOG4105C6T; Bacteria.
DR   eggNOG; COG0031; LUCA.
DR   HOGENOM; HOG000217394; -.
DR   KO; K12339; -.
DR   OMA; FTTTGPE; -.
DR   Proteomes; UP000000815; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005858; CysM.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
DR   PANTHER; PTHR10314:SF145; PTHR10314:SF145; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01136; cysKM; 1.
DR   TIGRFAMs; TIGR01138; cysM; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000815};
KW   Cysteine biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW   ECO:0000256|RuleBase:RU003985};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000815};
KW   Transferase {ECO:0000256|RuleBase:RU003985,
KW   ECO:0000313|EMBL:CAL21614.1}.
FT   REGION      174    178       Pyridoxal phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR605856-50}.
FT   BINDING      71     71       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   BINDING     255    255       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR605856-51}.
SQ   SEQUENCE   292 AA;  31279 MW;  569CDEA6B4BE6721 CRC64;
     MTTLEHCIGH TPLVKLQRLS QGLNAEIWVK LEGNNPAGSV KDRAALAMIQ QAELRGDIAP
     GDVLIEATSG NTGIALAMIA AMKGYHLKLL MPENMSQERQ AAMRAYGAEL ILVSREQGME
     GARDLALTMQ ENGEGNVLDQ FNNADNPYAH FTGTGPEIWQ QTAGKVSHFV SSMGTTGTIT
     GVSQYLKSQN PQVKVIGLQP AEGSSIPGIR RWSAEYIPGI FRPELVDQVL DITQSVAEQT
     MRRLAKEEGI FCGVSSGGAV AGALRIAADN PDAVIVAIIC DRGDRYLSTG VF
//
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