ID   CYSM_MYCTO              Reviewed;         323 AA.
AC   P9WP52; L0T934; P63873; Q10624;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=O-phosphoserine sulfhydrylase;
DE            Short=OPS sulfhydrylase;
DE            EC=2.5.1.113 {ECO:0000250|UniProtKB:P9WP53};
DE   AltName: Full=CysO-thiocarboxylate-dependent cysteine synthase;
DE   AltName: Full=Cysteine synthase B;
DE            Short=CSase B;
DE   AltName: Full=O-phosphoserine-specific cysteine synthase;
DE   AltName: Full=[CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase;
GN   Name=cysM; OrderedLocusNames=MT1377;
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 formation of a covalent CysO-cysteine adduct
CC       via a sulfur transfer, using the thiocarboxylated sulfur carrier
CC       protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as
CC       sulfur acceptor. May be of particular importance for cysteine
CC       biosynthesis in the persistent phase of M.tuberculosis.
CC       {ECO:0000250|UniProtKB:P9WP53}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + O-phospho-L-
CC         serine = [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-Cys +
CC         phosphate; Xref=Rhea:RHEA:48740, Rhea:RHEA-COMP:12207, Rhea:RHEA-
CC         COMP:12213, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:90783; EC=2.5.1.113;
CC         Evidence={ECO:0000250|UniProtKB:P9WP53};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P9WP53};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WP53}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45642.1; -; Genomic_DNA.
DR   PIR; D70771; D70771.
DR   RefSeq; WP_003406912.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP52; -.
DR   SMR; P9WP52; -.
DR   EnsemblBacteria; AAK45642; AAK45642; MT1377.
DR   GeneID; 45425314; -.
DR   KEGG; mtc:MT1377; -.
DR   PATRIC; fig|83331.31.peg.1485; -.
DR   HOGENOM; CLU_021018_1_0_11; -.
DR   UniPathway; UPA00136; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
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; 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; 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..323
FT                   /note="O-phosphoserine sulfhydrylase"
FT                   /id="PRO_0000427012"
FT   BINDING         81
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..188
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  34438 MW;  B743231FEFA87573 CRC64;
     MTRYDSLLQA LGNTPLVGLQ RLSPRWDDGR DGPHVRLWAK LEDRNPTGSI KDRPAVRMIE
     QAEADGLLRP GATILEPTSG NTGISLAMAA RLKGYRLICV MPENTSVERR QLLELYGAQI
     IFSAAEGGSN TAVATAKELA ATNPSWVMLY QYGNPANTDS HYCGTGPELL ADLPEITHFV
     AGLGTTGTLM GTGRFLREHV ANVKIVAAEP RYGEGVYALR NMDEGFVPEL YDPEILTARY
     SVGAVDAVRR TRELVHTEGI FAGISTGAVL HAALGVGAGA LAAGERADIA LVVADAGWKY
     LSTGAYAGSL DDAETALEGQ LWA