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Database: UniProt/SWISS-PROT
Entry: PNCB_XANC8
LinkDB: PNCB_XANC8
Original site: PNCB_XANC8 
ID   PNCB_XANC8              Reviewed;         398 AA.
AC   Q4UQS8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-JUN-2014, entry version 58.
DE   RecName: Full=Nicotinate phosphoribosyltransferase;
DE            Short=NAPRTase;
DE            EC=6.3.4.21;
GN   Name=pncB; OrderedLocusNames=XC_3552;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L.,
RA   Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA   Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
CC   -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-
CC       ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate
CC       at the expense of ATP (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nicotinate + 5-phospho-alpha-D-ribose 1-
CC       diphosphate + ATP + H(2)O = beta-nicotinate D-ribonucleotide +
CC       diphosphate + ADP + phosphate.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
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DR   EMBL; CP000050; AAY50595.1; -; Genomic_DNA.
DR   RefSeq; YP_244615.1; NC_007086.1.
DR   ProteinModelPortal; Q4UQS8; -.
DR   STRING; 314565.XC_3552; -.
DR   EnsemblBacteria; AAY50595; AAY50595; XC_3552.
DR   GeneID; 3379167; -.
DR   KEGG; xcb:XC_3552; -.
DR   PATRIC; 24068801; VBIXanCam24967_3762.
DR   eggNOG; COG1488; -.
DR   HOGENOM; HOG000284928; -.
DR   KO; K00763; -.
DR   OMA; QAVFHRY; -.
DR   OrthoDB; EOG6X10XB; -.
DR   BioCyc; XCAM314565:GCQG-3579-MONOMER; -.
DR   UniPathway; UPA00253; UER00457.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019357; P:nicotinate nucleotide biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00570; NAPRTase; 1.
DR   InterPro; IPR006406; Nic_PRibTrfase.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   Pfam; PF04095; NAPRTase; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR01514; NAPRTase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ligase; Pyridine nucleotide biosynthesis;
KW   Transferase.
FT   CHAIN         1    398       Nicotinate phosphoribosyltransferase.
FT                                /FTId=PRO_1000025019.
SQ   SEQUENCE   398 AA;  45452 MW;  B32734C0571FEC82 CRC64;
     MIIHSLLDTD LYKFTMMQAV LHQHPAAQVD YRFKCRTPGV DLAQFIDEIS REIDALCRLR
     LREDEVDYLR SLRFIKPDFA DFLALFHLDR KYLALAASAA HPGEIELTIR GPWLHTILFE
     VPLLAIINEV WFRNTSEPDF EEGRSRLREK VRSLRSMPAG CKIADYGTRR RYSRQWHGEL
     LPLLRDGLGE QFVGTSNVFF AKQYGLTPLG TMAHEYLQAF QALGPRLRDS QVAALDSWAR
     EYRGDLGIAL SDVVGLDAFL RDFDLYFCKL FDGMRHDSGD PFDWGERVIA HLEAHRVDPR
     TKVLVFSDGL NIDKVMRLYE HFSPRCRLAF GVGTSLTNDL GPTPLQIVIK MVRCNGQPVA
     KLSDSPGKSM CEDLGYLRYL RDVFGLPPMP EAGDPARQ
//
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