ID   CYSK_MYCTO              Reviewed;         310 AA.
AC   P9WP54; L0TC08; P0A534; P95230;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=O-acetylserine sulfhydrylase;
DE            Short=OAS sulfhydrylase;
DE            Short=OASS;
DE            EC=2.5.1.47;
DE   AltName: Full=Cysteine synthase A;
DE            Short=CSase A;
DE   AltName: Full=O-acetylserine (thiol)-lyase A;
DE            Short=OAS-TL A;
DE   AltName: Full=O-acetylserine-specific cysteine synthase;
DE   AltName: Full=Sulfide-dependent cysteine synthase;
GN   Name=cysK1; Synonyms=cysK; OrderedLocusNames=MT2397;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the conversion of O-acetylserine (OAS) to cysteine
CC       through the elimination of acetate and addition of hydrogen sulfide.
CC       {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK46689.1; -; Genomic_DNA.
DR   PIR; G70660; G70660.
DR   RefSeq; WP_003899275.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP54; -.
DR   SMR; P9WP54; -.
DR   EnsemblBacteria; AAK46689; AAK46689; MT2397.
DR   GeneID; 45426318; -.
DR   KEGG; mtc:MT2397; -.
DR   PATRIC; fig|83331.31.peg.2585; -.
DR   HOGENOM; CLU_021018_1_0_11; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000001020; 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="O-acetylserine sulfhydrylase"
FT                   /id="PRO_0000427011"
FT   BINDING         74
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..182
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         44
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  32753 MW;  597B1106CA6D0B9A CRC64;
     MSIAEDITQL IGRTPLVRLR RVTDGAVADI VAKLEFFNPA NSVKDRIGVA MLQAAEQAGL
     IKPDTIILEP TSGNTGIALA MVCAARGYRC VLTMPETMSL ERRMLLRAYG AELILTPGAD
     GMSGAIAKAE ELAKTDQRYF VPQQFENPAN PAIHRVTTAE EVWRDTDGKV DIVVAGVGTG
     GTITGVAQVI KERKPSARFV AVEPAASPVL SGGQKGPHPI QGIGAGFVPP VLDQDLVDEI
     ITVGNEDALN VARRLAREEG LLVGISSGAA TVAALQVARR PENAGKLIVV VLPDFGERYL
     STPLFADVAD