ID   CYSK_MYCLE              Reviewed;         310 AA.
AC   O32978;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=cysK; OrderedLocusNames=ML0839; ORFNames=MLCB22.47;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
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DR   EMBL; Z98741; CAB11412.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30349.1; -; Genomic_DNA.
DR   PIR; T44912; T44912.
DR   RefSeq; NP_301633.1; NC_002677.1.
DR   RefSeq; WP_010907957.1; NC_002677.1.
DR   AlphaFoldDB; O32978; -.
DR   SMR; O32978; -.
DR   STRING; 272631.ML0839; -.
DR   EnsemblBacteria; CAC30349; CAC30349; CAC30349.
DR   KEGG; mle:ML0839; -.
DR   PATRIC; fig|272631.5.peg.1554; -.
DR   Leproma; ML0839; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_021018_1_0_11; -.
DR   OMA; FWDSGER; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000000806; 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="O-acetylserine sulfhydrylase"
FT                   /id="PRO_0000167093"
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;  32661 MW;  6D94127327ABCB36 CRC64;
     MSIAEDVTQL VGNTPLVRLR RVTEGALADV VAKLESFNPA NSVKDRIGVA MIDTAEEAGL
     IKPDTVILEP TSGNTGIALA MVCAARGYHC VLTMPETMSI ERRMLLRAYG AELILTPGAD
     GMSGAIAKAE ELAKSDKRYF IPQQFENPAN PAIHAATTAE EVWRDTDGKV DIFVSGIGTG
     GTITGVARII KERRPATQFV AVEPAASPVL SGGQKGPHPI QGIGAGFVPS VLVLDLVDEI
     VTVGNEEALD LARRLAKEEG LLVGISAGAA VCAALHVARR PENTGKLIVV VLPDFGERYL
     STMLFADLAN