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Database: UniProt/SWISS-PROT
Entry: PNCB_SHIBS
LinkDB: PNCB_SHIBS
Original site: PNCB_SHIBS 
ID   PNCB_SHIBS              Reviewed;         400 AA.
AC   Q31YR6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   01-MAY-2013, entry version 51.
DE   RecName: Full=Nicotinate phosphoribosyltransferase;
DE            Short=NAPRTase;
DE            EC=2.4.2.11;
GN   Name=pncB; OrderedLocusNames=SBO_2222;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- CATALYTIC ACTIVITY: Beta-nicotinate D-ribonucleotide + diphosphate
CC       = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
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DR   EMBL; CP000036; ABB66792.1; -; Genomic_DNA.
DR   RefSeq; YP_408620.1; NC_007613.1.
DR   HSSP; P39683; 1VLP.
DR   ProteinModelPortal; Q31YR6; -.
DR   SMR; Q31YR6; 3-385.
DR   STRING; 300268.SBO_2222; -.
DR   EnsemblBacteria; ABB66792; ABB66792; SBO_2222.
DR   GeneID; 3781205; -.
DR   KEGG; sbo:SBO_2222; -.
DR   PATRIC; 18683765; VBIShiBoy33460_2801.
DR   eggNOG; COG1488; -.
DR   HOGENOM; HOG000284928; -.
DR   KO; K00763; -.
DR   OMA; SFGWGTN; -.
DR   ProtClustDB; PRK05321; -.
DR   BioCyc; SBOY300268:GJFL-2219-MONOMER; -.
DR   UniPathway; UPA00253; UER00457.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:HAMAP.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP.
DR   GO; GO:0019357; P:nicotinate nucleotide biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00570; NAPRTase; 1; -.
DR   InterPro; IPR006406; Nic_PRibTrfase.
DR   InterPro; IPR015977; Nic_PRibTrfase-like.
DR   InterPro; IPR007229; Nic_PRibTrfase-rel.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   PANTHER; PTHR11098:SF1; PTHR11098:SF1; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; Q_phspho_trans; 1.
DR   TIGRFAMs; TIGR01514; NAPRTase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycosyltransferase;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN         1    400       Nicotinate phosphoribosyltransferase.
FT                                /FTId=PRO_1000025011.
SQ   SEQUENCE   400 AA;  45911 MW;  5385BCB1A8703095 CRC64;
     MTQFASPVLH SLLDTDAYKL HMQQAVFHHY YDVHVAAEFR CRGDDLLGIY ADAIREQIQA
     MQHLRLQDDE YQWLSALPFF KADYLNWLRE FRFNPEQVTV SNDNGKLDIR LSGPWREVIL
     WEVPLLAVIS EMVHRYRSPQ ADVAQALDTL ESKLVDFSAL TAGLDMSRFH LMDFGTRRRF
     SREVQETIVK RLQQESWFVG TSNYDLARRL SLTPMGTQAH EWFQAHQQIS PDLANSQRAA
     LAAWLEEYPD QLGIALTDCI TMDAFLRDFG VEFASRYQGL RHDSGDPVEW GEKAIAHYEK
     LGIDPQSKTL VFSDNLDLRK AVELYRHFSS RVQLSFGIGT RLTCDIPQVK PLNIVIKLVE
     CNGKPVAKLS DSPGKTICHD KAFVRALRKA FDLPHIKKAS
//
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