(data stored in ACNUC7421 zone)

SWISSPROT: PNCB_PSEPF

ID   PNCB_PSEPF              Reviewed;         407 AA.
AC   Q3KIW4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00570};
DE            Short=NAPRTase {ECO:0000255|HAMAP-Rule:MF_00570};
DE            EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570};
GN   Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570};
GN   OrderedLocusNames=Pfl01_0548;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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. {ECO:0000255|HAMAP-Rule:MF_00570}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC         nicotinate = ADP + diphosphate + nicotinate beta-D-
CC         ribonucleotide + phosphate; Xref=Rhea:RHEA:36163,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:32544,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:456216; EC=6.3.4.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00570};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00570}.
CC   -!- PTM: Transiently phosphorylated on a His residue during the
CC       reaction cycle. Phosphorylation strongly increases the affinity
CC       for substrates and increases the rate of nicotinate D-
CC       ribonucleotide production. Dephosphorylation regenerates the low-
CC       affinity form of the enzyme, leading to product release.
CC       {ECO:0000255|HAMAP-Rule:MF_00570}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00570}.
DR   EMBL; CP000094; ABA72292.1; -; Genomic_DNA.
DR   RefSeq; WP_011332202.1; NC_007492.2.
DR   SMR; Q3KIW4; -.
DR   STRING; 205922.Pfl01_0548; -.
DR   PRIDE; Q3KIW4; -.
DR   EnsemblBacteria; ABA72292; ABA72292; Pfl01_0548.
DR   KEGG; pfo:Pfl01_0548; -.
DR   eggNOG; ENOG4107RH7; Bacteria.
DR   eggNOG; COG1488; LUCA.
DR   HOGENOM; HOG000284928; -.
DR   KO; K00763; -.
DR   OMA; GTSNVHF; -.
DR   BioCyc; PFLU205922:G1G4S-555-MONOMER; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019357; P:nicotinate nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01401; PncB_like; 1.
DR   HAMAP; MF_00570; NAPRTase; 1.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR006406; Nic_PRibTrfase.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   PANTHER; PTHR11098; PTHR11098; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR01514; NAPRTase; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KIW4.
DR   SWISS-2DPAGE; Q3KIW4.
KW   Complete proteome; Ligase; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    407       Nicotinate phosphoribosyltransferase.
FT                                /FTId=PRO_1000025007.
FT   MOD_RES     224    224       Phosphohistidine; by autocatalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00570}.
SQ   SEQUENCE   407 AA;  46872 MW;  3194946C703E7918 CRC64;
     MSESVFADRI VQNLLDTDFY KLTMMQAVLH NYPNVEVEWE FRCRNSEDLR PYLAEIRFQV
     ERLAELSLSA DQLSFLERIS FLKPDFLRFL GLFRFNLRYL HTGIENGELF IRLRGPWLHV
     ILFEVPLLAI VSEVRNRYRY RETVLEQARE QLYRKFDWLT ANASAEELSQ LQVADFGTRR
     RFSYRVQEEV VNVLKHDFPG RFVGTSNVHL SRELDMKPLG TMAHEWIMAH QQLGPRLIDS
     QIAALDCWVR EYRGLLGIAL TDCITTDAFL GDFDLFFAKL FDGLRHDSGD PVLWGEKCIA
     HYHKLGIDPM SKTLVFSDSL TLPKSLEIFR ALRGRINVSF GIGTNLTCDI PGVEPMSIVL
     KMTACNGQPV AKISDEPGKT HCKDPNFVAY LRHVFQVPAV SSLSSKE
//

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