(data stored in ACNUC7421 zone)

SWISSPROT: B7UIF7_ECO27

ID   B7UIF7_ECO27            Unreviewed;       297 AA.
AC   B7UIF7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   SubName: Full=Quinolinate phosphoribosyltransferase {ECO:0000313|EMBL:CAS07660.1};
GN   Name=nadC {ECO:0000313|EMBL:CAS07660.1};
GN   OrderedLocusNames=E2348C_0112 {ECO:0000313|EMBL:CAS07660.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07660.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07660.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|PIRNR:PIRNR006250}.
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DR   EMBL; FM180568; CAS07660.1; -; Genomic_DNA.
DR   RefSeq; WP_001135168.1; NC_011601.1.
DR   SMR; B7UIF7; -.
DR   EnsemblBacteria; CAS07660; CAS07660; E2348C_0112.
DR   KEGG; ecg:E2348C_0112; -.
DR   HOGENOM; HOG000224022; -.
DR   KO; K00767; -.
DR   OMA; CGGCHNH; -.
DR   BioCyc; ECOL574521:E2348C_RS00580-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   CDD; cd01572; QPRTase; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.90.1170.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004393; NadC.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   PANTHER; PTHR32179; PTHR32179; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR00078; nadC; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIF7.
DR   SWISS-2DPAGE; B7UIF7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR006250,
KW   ECO:0000313|EMBL:CAS07660.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006250,
KW   ECO:0000313|EMBL:CAS07660.1}.
FT   DOMAIN       43    129       QRPTase_N. {ECO:0000259|Pfam:PF02749}.
FT   DOMAIN      131    295       QRPTase_C. {ECO:0000259|Pfam:PF01729}.
FT   REGION      152    154       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   REGION      259    261       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   REGION      280    282       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   BINDING     119    119       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   BINDING     176    176       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   BINDING     186    186       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   BINDING     215    215       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
FT   BINDING     236    236       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006250-1}.
SQ   SEQUENCE   297 AA;  32772 MW;  A45E68804A7B2024 CRC64;
     MPPRRYNPDT RRDELLERIN LDIPGAVAQA LREDLGGTVD ANNDITAKLL PENSRSHATV
     ITRENGVFCG KRWVEEVFIQ LAGDDVTIIW HVDDGDVINA NQPLFELEGP SRVLLTGERT
     ALNFVQTLSG VASKVRHYVE LLEGTNTQLL DTRKTLPGLR SALKYAVLCG GGANHRLGLS
     DAFLIKENHI IASGSVRQAV EKASWLHPDA PVEVEVENLE ELDEALKAGA DIIMLDNFET
     EQMREAVKRT NGKALLEVSG NVTDKTLREF AETGVDFISV GALTKHVQAL DLSMRFR
//

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