ID   PNCB_BRASO              Reviewed;         434 AA.
AC   A4YK54;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=BRADO0323;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CU234118; CAL74280.1; -; Genomic_DNA.
DR   RefSeq; WP_011923561.1; NC_009445.1.
DR   AlphaFoldDB; A4YK54; -.
DR   SMR; A4YK54; -.
DR   STRING; 114615.BRADO0323; -.
DR   PRIDE; A4YK54; -.
DR   EnsemblBacteria; CAL74280; CAL74280; BRADO0323.
DR   KEGG; bra:BRADO0323; -.
DR   eggNOG; COG1488; Bacteria.
DR   HOGENOM; CLU_030991_1_0_5; -.
DR   OMA; QAVFHRY; -.
DR   OrthoDB; 241792at2; -.
DR   BioCyc; BSP114615:BRADO_RS01540-MON; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001994; 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   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;
KW   Reference proteome.
FT   CHAIN           1..434
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_1000146834"
FT   MOD_RES         242
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   434 AA;  49506 MW;  23B98C80298AFC4D CRC64;
     MTVTDIASRT YNHGWRLDPI VRSLLDTDFY KLLMLQMIRE FYPDQKVTFS VINRTKRVRL
     GDVIDEGELR AQLDHARTIR FSKKELIWLA GNTFYGKTHM FSPDFLAWLA NFRLPEYELH
     KADGQYELHF HGLWTHTTMW EIPALAIVNE LRSRQAMKGQ GRFALDVLFA RAKAKLWAKV
     ERLRKLEGLR LSDFGTRRRH GFLWQRWCVE AVKEGLGSSF TGTSNVLLAM DNDLEAIGTN
     AHELPMVAAA LAKDDDELRF APYRILDQWR QTYAGNLLIA LPDAFGTKAF LRDAPDWVAD
     WTGFRPDSAP PIQAGEEIIA WWKSKGRDPR QKLLVFSDAM DVESIEQIHQ RFSDQVRLSF
     GWGTNLTNDF VGCSPDGSVD LDPISLVCKV TSVDGRPAVK LSDNPEKATG DPAEIARYLR
     VFGDAGRVRT PVFV