ID   CYSK_STAAM              Reviewed;         310 AA.
AC   P63870; Q99W90;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SAV0513;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB56675.1; -; Genomic_DNA.
DR   RefSeq; WP_000057594.1; NC_002758.2.
DR   AlphaFoldDB; P63870; -.
DR   SMR; P63870; -.
DR   World-2DPAGE; 0002:P63870; -.
DR   PaxDb; P63870; -.
DR   EnsemblBacteria; BAB56675; BAB56675; SAV0513.
DR   KEGG; sav:SAV0513; -.
DR   HOGENOM; CLU_021018_1_0_9; -.
DR   OMA; FWDSGER; -.
DR   PhylomeDB; P63870; -.
DR   BioCyc; SAUR158878:SAV_RS02815-MON; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000002481; 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   Transferase.
FT   CHAIN           1..310
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167096"
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;  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