ID   CYSK_FLAS3              Reviewed;         307 AA.
AC   Q59447;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
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;
OS   Flavobacterium sp. (strain K3-15 / DSM ID92-509).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium; unclassified Flavobacterium.
OX   NCBI_TaxID=268949;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8867384; DOI=10.1111/j.1574-6968.1996.tb08065.x;
RA   Mueller R., Kuttler E., Lanz C., Drewks C., Schmidt K.;
RT   "Isolation of a gene encoding cysteine synthase from Flavobacterium K3-
RT   15.";
RL   FEMS Microbiol. Lett. 136:305-308(1996).
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   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; Z50729; CAA90597.1; -; Genomic_DNA.
DR   PIR; S58299; S58299.
DR   AlphaFoldDB; Q59447; -.
DR   SMR; Q59447; -.
DR   UniPathway; UPA00136; UER00200.
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..307
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167091"
FT   BINDING         72
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         176..180
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  33340 MW;  5A1D8199718BF2BD CRC64;
     MKFQNALETI GNTPVVKINN LFNSDHEIWI KLEKSNPGGS IKDRIALAMI EDAEAKGLLN
     KDSTIIEPTS GNTGIGLALV AAVKGYKLIL VMPESMSIER RKIMEAYGAE FVLTPREKGM
     KGAIEKANEL AEETPNSWIP RQFDNPANVK IHVETTAQEI LQDFPEGLDY VITGVGTGGH
     ITGIAKALKE KYPNLKVIAV EPELSPVLSG GSPAPHPLQG LGAGFVPSIL DITLLDGVIT
     VGKDEAYEYA INAAKKEGLF CGSFHRSRLS RYRKTFTGNT AWSKNSLPLI TTPEKGIFLL
     RDSSKIL