ID   CYSK_STAEQ              Reviewed;         310 AA.
AC   Q5HRP1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=SERP0152;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
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., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; CP000029; AAW53521.1; -; Genomic_DNA.
DR   RefSeq; WP_001832242.1; NC_002976.3.
DR   AlphaFoldDB; Q5HRP1; -.
DR   SMR; Q5HRP1; -.
DR   STRING; 176279.SERP0152; -.
DR   EnsemblBacteria; AAW53521; AAW53521; SERP0152.
DR   GeneID; 50019576; -.
DR   KEGG; ser:SERP0152; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_021018_1_0_9; -.
DR   OMA; FWDSGER; -.
DR   OrthoDB; 1033353at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000000531; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
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; Cysteine biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..310
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167102"
FT   BINDING         76
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..184
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  33152 MW;  E231BA75F40A63EE CRC64;
     MAQKPVDYVT QIIGNTPVVK LRNVVDDDAA DIYVKLEYQN PGGSVKDRIA LAMIEKAERE
     GKIKPGDTIV EPTSGNTGIG LAFVCAAKGY KAVFTMPETM SQERRNLLKA YGAELVLTPG
     SEAMKGAIKK AKELKEEHGY FEPQQFENPA NPEIHELTTG PELVEQFEGR QIDAFLAGVG
     TGGTLSGVGK VLKKEYPNVE IVAIEPEASP VLSGGEPGPH KLQGLGAGFV PDTLNTEVYD
     SIIKVGNDTA MDMARRVARE EGILAGISSG AAIYAAIQKA KELGKGKTVV TVLPSNGERY
     LSTPLYSFDN