ID   CYSK_STAHA              Reviewed;         155 AA.
AC   Q59918;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
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;
DE   Flags: Fragment;
GN   Name=cysK;
OS   Staphylococcus haemolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8586264; DOI=10.1111/j.1574-6968.1995.tb07932.x;
RA   Kellam P., Dallas W.S., Ballantine S.P., Delves C.J.;
RT   "Functional cloning of the dihydropteroate synthase gene of Staphylococcus
RT   haemolyticus.";
RL   FEMS Microbiol. Lett. 134:165-169(1995).
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; U40768; AAC43582.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59918; -.
DR   SMR; Q59918; -.
DR   STRING; 1283.ShL2_02283; -.
DR   UniPathway; UPA00136; UER00200.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1100; -; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           <1..155
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167103"
FT   BINDING         25..29
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   155 AA;  16121 MW;  609CF880E5826BBA CRC64;
     ELTTGPEIVE QFEGKQIDAF LAGVGTGGTL SGAGKVLKEK YPNIEIVAIE PEASPVLSGG
     EPGPHKLQGL GAGFVPDTLN TDIYDSIIQV GNDIAMETSR RVAKEEGILA GISSGAAIHA
     AIQKAKELGK GKTVLTVLPS NGERYLSTPL YSFDD