ID   PNCB_RALPJ              Reviewed;         389 AA.
AC   B2U8V2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 91.
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}; OrderedLocusNames=Rpic_0896;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide
CC       from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of
CC       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-ribonucleotide +
CC         phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:456216; EC=6.3.4.21; Evidence={ECO:0000255|HAMAP-
CC         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 reaction
CC       cycle. Phosphorylation strongly increases the affinity for substrates
CC       and increases the rate of nicotinate D-ribonucleotide production.
CC       Dephosphorylation regenerates the low-affinity form of the enzyme,
CC       leading to product release. {ECO:0000255|HAMAP-Rule:MF_00570}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00570}.
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DR   EMBL; CP001068; ACD26046.1; -; Genomic_DNA.
DR   RefSeq; WP_012435213.1; NC_010682.1.
DR   AlphaFoldDB; B2U8V2; -.
DR   SMR; B2U8V2; -.
DR   STRING; 402626.Rpic_0896; -.
DR   EnsemblBacteria; ACD26046; ACD26046; Rpic_0896.
DR   KEGG; rpi:Rpic_0896; -.
DR   PATRIC; fig|402626.5.peg.2096; -.
DR   eggNOG; COG1488; Bacteria.
DR   HOGENOM; CLU_030991_1_0_4; -.
DR   OMA; QAVFHRY; -.
DR   OrthoDB; 241792at2; -.
DR   UniPathway; UPA00253; UER00457.
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   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;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis.
FT   CHAIN           1..389
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_1000129479"
FT   MOD_RES         216
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   389 AA;  44841 MW;  DAD25AA8D17CDEDF CRC64;
     MIIRSLLDTD LYKFTMMQVV LHHFPGAHVE YRFKCRNAGV DLVPFIEEIR AEIRHLCTLR
     FTDTELDYLR GMRFIKSDFV DFLGLFHLNE KYIDVRPAPS NDGQIEIVIA GPWLHTIMFE
     VPVLAIVNEV FFSRTQTHPQ WEEGKRRLTD KLASLKRPGL EDCRIADYGT RRRFSHTWHE
     HVLLETHAQL GAQYAGTSNV YFAMKHGMTP LGTMAHEYLQ ACQALGPRLR DSQTFALETW
     AKEYRGDLGI ALSDTYGFDA FLRDFDMFFC KLFDGVRHDS GDPFEWGERM LKHYDDMRAE
     PKSKALIFSD SLDMPKVIGL YERFHGRCKL AFGVGTNLTN DLGYTPLQIV IKIVRCNGQP
     VAKLSDAPEK TMCDDPAYLT YLKQVFGVQ