ID   CYSM_CAMJE              Reviewed;         299 AA.
AC   P71128; Q0P9Y7; Q9PP20;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Cysteine synthase B;
DE            Short=CSase B;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase B;
DE            Short=OAS-TL B;
DE   AltName: Full=O-acetylserine sulfhydrylase B;
GN   Name=cysM; OrderedLocusNames=Cj0912c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F38011;
RX   PubMed=9034314; DOI=10.1016/s0378-1119(96)00631-2;
RA   Garvis S.G., Tipton S.L., Konkel M.E.;
RT   "Identification of a functional homolog of the Escherichia coli and
RT   Salmonella typhimurium cysM gene encoding O-acetylserine sulfhydrylase B in
RT   Campylobacter jejuni.";
RL   Gene 185:63-67(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate;
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   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; U63157; AAC44853.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL35032.1; -; Genomic_DNA.
DR   PIR; G81364; G81364.
DR   PIR; JC6185; JC6185.
DR   RefSeq; WP_002858759.1; NC_002163.1.
DR   RefSeq; YP_002344310.1; NC_002163.1.
DR   AlphaFoldDB; P71128; -.
DR   SMR; P71128; -.
DR   STRING; 192222.Cj0912c; -.
DR   PaxDb; 192222-Cj0912c; -.
DR   EnsemblBacteria; CAL35032; CAL35032; Cj0912c.
DR   GeneID; 906009; -.
DR   KEGG; cje:Cj0912c; -.
DR   PATRIC; fig|192222.6.peg.896; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_021018_1_0_7; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   FunFam; 3.40.50.1100:FF:000006; Cysteine synthase; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR050214; Cys_Synth/Cystath_Beta-Synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-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   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..299
FT                   /note="Cysteine synthase B"
FT                   /id="PRO_0000167107"
FT   BINDING         70
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..178
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        87
FT                   /note="I -> V (in Ref. 1; AAC44853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="R -> K (in Ref. 1; AAC44853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="E -> Q (in Ref. 1; AAC44853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="S -> I (in Ref. 1; AAC44853)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  32385 MW;  8298782DA1852ACB CRC64;
     MKVHEKVSEL IGNTPIIHLK KFGINVFAKC EFLNPSHSIK DRAAFEMIKD ALDSKKINQD
     TTIVEATSGN TGISLAMICA DLGLKFIAVM PESMSLERRK MITLFGARLE LTPANLGMKG
     AVDKANEILL NTPNSFMVSQ FENISNKNAH RKNTALEILR DLDNELDIFV AGFGTGGTIS
     GVGEILKEKL EKVHIVGVEP LNSPLLSKGE AGSHKIQGIG ANFIPAILNK EVIDEVITVS
     NEDAINTAKE LAKSGLMVGI SSGANVFAAS MLAKKFPDKR ILTMLNDTAE RYLSTDLFA
//