ID   CYSM_MYCBO              Reviewed;         323 AA.
AC   P63874; A0A1R3XZ12; Q10624; X2BHT6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=BQ2027_MB1371;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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. Can also use sodium sulfide as sulfur donor in vitro,
CC       albeit with less efficiency. {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   -!- DOMAIN: The five C-terminal amino acid residues are inserted into the
CC       active site cleft in the closed conformation, protect the aminoacrylate
CC       intermediate and are involved in sulfur donor selectivity.
CC       {ECO:0000250|UniProtKB:P9WP53}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; LT708304; SIT99974.1; -; Genomic_DNA.
DR   RefSeq; NP_855025.1; NC_002945.3.
DR   RefSeq; WP_003406912.1; NC_002945.4.
DR   AlphaFoldDB; P63874; -.
DR   SMR; P63874; -.
DR   EnsemblBacteria; SIT99974; SIT99974; BQ2027_MB1371.
DR   GeneID; 45425314; -.
DR   PATRIC; fig|233413.5.peg.1503; -.
DR   OMA; GIRRWPE; -.
DR   UniPathway; UPA00136; -.
DR   Proteomes; UP000001419; 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_0000167113"
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                   /evidence="ECO:0000250"
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