ID CYSK_STAAC Reviewed; 310 AA.
AC Q5HIG2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 59.
DE RecName: Full=Cysteine synthase;
DE Short=CSase;
DE EC=2.5.1.47;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OAS-TL;
DE AltName: Full=O-acetylserine sulfhydrylase;
GN Name=cysK; OrderedLocusNames=SACOL0557;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete
RT genome analysis of an early methicillin-resistant Staphylococcus
RT aureus strain and a biofilm-producing methicillin-resistant
RT Staphylococcus epidermidis strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- CATALYTIC ACTIVITY: O(3)-acetyl-L-serine + H(2)S = L-cysteine +
CC acetate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
CC cysteine from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family.
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DR EMBL; CP000046; AAW37669.1; -; Genomic_DNA.
DR RefSeq; YP_185445.1; NC_002951.2.
DR ProteinModelPortal; Q5HIG2; -.
DR SMR; Q5HIG2; 4-310.
DR STRING; 93062.SACOL0557; -.
DR EnsemblBacteria; AAW37669; AAW37669; SACOL0557.
DR GeneID; 3237125; -.
DR KEGG; sac:SACOL0557; -.
DR PATRIC; 19527360; VBIStaAur112458_0542.
DR eggNOG; COG0031; -.
DR HOGENOM; HOG000217394; -.
DR KO; K01738; -.
DR OMA; KDRIAIS; -.
DR ProtClustDB; CLSK884704; -.
DR UniPathway; UPA00136; UER00200.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR InterPro; IPR001216; Cys_synth_BS.
DR InterPro; IPR005856; Cys_synthKM.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1.
DR TIGRFAMs; TIGR01139; cysK; 1.
DR TIGRFAMs; TIGR01136; cysKM; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1 310 Cysteine synthase.
FT /FTId=PRO_0000167095.
FT REGION 180 184 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 76 76 Pyridoxal phosphate (By similarity).
FT BINDING 268 268 Pyridoxal phosphate (By similarity).
FT MOD_RES 46 46 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 310 AA; 32976 MW; B881E3E85FF0DBC3 CRC64;
MAQKPVDNIT QIIGGTPVVK LRNVVDDNAA DVYVKLEYQN PGGSVKDRIA LAMIEKAERE
GKIKPGDTIV EPTSGNTGIG LAFVCAAKGY KAVFTMPETM SQERRNLLKA YGAELVLTPG
SEAMKGAIKK AKELKEEHGY FEPQQFENPA NPEVHELTTG PELLQQFEGK TIDAFLAGVG
TGGTLSGVGK VLKKEYPNIE IVAIEPEASP VLSGGEPGPH KLQGLGAGFI PGTLNTEIYD
SIIKVGNDTA MEMSRRVAKE EGILAGISSG AAIYAAIQKA KELGKGKTVV TVLPSNGERY
LSTPLYSFDD
//
