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Database: UniProt
Entry: Q5HIG2
LinkDB: Q5HIG2
Original site: Q5HIG2 
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   11-JUN-2014, entry version 64.
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-acetyl-L-serine + hydrogen sulfide = L-
CC       cysteine + 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; VKCRIGS; -.
DR   OrthoDB; EOG6Q2SP8; -.
DR   BioCyc; SAUR93062:GCEP-547-MONOMER; -.
DR   UniPathway; UPA00136; UER00200.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-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; SSF53686; 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
//
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