ID   PNCB_BUCAT              Reviewed;         399 AA.
AC   B8D7P8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=BUAPTUC7_355;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001158; ACL30163.1; -; Genomic_DNA.
DR   RefSeq; WP_009874317.1; NC_011834.1.
DR   AlphaFoldDB; B8D7P8; -.
DR   SMR; B8D7P8; -.
DR   KEGG; bau:BUAPTUC7_355; -.
DR   HOGENOM; CLU_030991_1_0_6; -.
DR   OMA; QAVFHRY; -.
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..399
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_1000146837"
FT   MOD_RES         221
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   399 AA;  46751 MW;  09A735641222EE19 CRC64;
     MKRYDYPIVK TLLDTDAYKL HMQQAVFYHY KNVNVVAEFL CRGDNFLGCY ANILLDQISM
     MRSLSLSHEE YVYMTSFPFF KKEYLHWLKK FRYNVSQVKI NSYQGRLHIR ISGLWKEVIL
     WEVPILALIS EVFHGNFSPE ITSQSALQYL DIKLKKFFNR TKYIDLSHLK IVDFGTRRRF
     SYDVQYSIVK RLKESFPFLI GSSNYHIARI LKIKPVGTQA HEWFQAHQQI GSNLKNSQIL
     ALQKWLYQYK NHLGIALTDS ITMDAFLDDF NLHFASFYQG IRHDSGDPVK WGEKALKHYE
     KLGIDPCTKT LLFSDNLDFK KIISLYKKFH KKINVIFGIG TKLTCDIPYV KPLNIVIKLV
     ECNGKPVAKI SDSPGKTFCL DRIFLKNLCQ VFNVSLKNR