CYSM_CAMJE
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 03-AUG-2022, entry version 131.
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 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC 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=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 -!- 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; P71128; -.
DR PRIDE; P71128; -.
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 OMA; FWDSGER; -.
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 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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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..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
