GenomeNet

Database: UniProt
Entry: P71128
LinkDB: P71128
Original site: P71128 
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   11-JUN-2014, entry version 98.
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 NCTC 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
RT   B in Campylobacter jejuni.";
RL   Gene 185:63-67(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., 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: O-acetyl-L-serine + hydrogen sulfide = L-
CC       cysteine + acetate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
CC       cysteine from L-serine: step 2/2.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U63157; AAC44853.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL35032.1; -; Genomic_DNA.
DR   PIR; G81364; G81364.
DR   PIR; JC6185; JC6185.
DR   RefSeq; YP_002344310.1; NC_002163.1.
DR   ProteinModelPortal; P71128; -.
DR   SMR; P71128; 4-295.
DR   STRING; 192222.Cj0912c; -.
DR   EnsemblBacteria; CAL35032; CAL35032; Cj0912c.
DR   GeneID; 906009; -.
DR   KEGG; cje:Cj0912c; -.
DR   PATRIC; 20058768; VBICamJej33762_0896.
DR   eggNOG; COG0031; -.
DR   HOGENOM; HOG000217394; -.
DR   KO; K01738; -.
DR   OMA; LLEENWP; -.
DR   OrthoDB; EOG6Q2SP8; -.
DR   BioCyc; CJEJ192222:GJTS-880-MONOMER; -.
DR   UniPathway; UPA00136; UER00200.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   InterPro; IPR001216; Cys_synth_BS.
DR   InterPro; IPR005856; Cys_synthKM.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
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; Complete proteome; Cysteine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN         1    299       Cysteine synthase B.
FT                                /FTId=PRO_0000167107.
FT   REGION      174    178       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      70     70       Pyridoxal phosphate (By similarity).
FT   BINDING     261    261       Pyridoxal phosphate (By similarity).
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   CONFLICT     87     87       I -> V (in Ref. 1; AAC44853).
FT   CONFLICT     99     99       R -> K (in Ref. 1; AAC44853).
FT   CONFLICT    235    235       E -> Q (in Ref. 1; AAC44853).
FT   CONFLICT    254    254       S -> I (in Ref. 1; AAC44853).
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
//
DBGET integrated database retrieval system