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 24-JAN-2024, entry version 44.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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}.
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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 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 CDD; cd01561; CBS_like; 1.
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; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01139; cysK; 1.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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_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
//
