ID   PNCB_SALAR              Reviewed;         400 AA.
AC   A9MHU8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=SARI_01957;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000880; ABX21838.1; -; Genomic_DNA.
DR   RefSeq; WP_012210305.1; NC_010067.1.
DR   AlphaFoldDB; A9MHU8; -.
DR   SMR; A9MHU8; -.
DR   STRING; 41514.SARI_01957; -.
DR   EnsemblBacteria; ABX21838; ABX21838; SARI_01957.
DR   KEGG; ses:SARI_01957; -.
DR   HOGENOM; CLU_030991_1_0_6; -.
DR   OMA; QAVFHRY; -.
DR   OrthoDB; 241792at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000002084; 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   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;
KW   Reference proteome.
FT   CHAIN           1..400
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_1000082327"
FT   MOD_RES         220
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   400 AA;  45841 MW;  088098AB83FE4CAE CRC64;
     MTQFASPVLH SLLDTDAYKL HMQQAVFHHY YDVQVAAEFR CRGDDLLGIY ADAIREQVDA
     MQHLRLQEDE FQWLSGLPFF KTDYLDWLRE FRYDPAQVCV TNDNGKLNIR LTGPWREVIM
     WEVPLLAVIS ELVHHYRSPK AGVDQALDAL ESKLVDFTAL TADLDMSRFH LMDFGTRRRF
     SREVQQTIVK RLQQEPWFVG TSNYDLARRL ALMPMGTQAH EWFQAHQQIS PDLATSQRAA
     LAAWLNEYPD QLGIALTDCI TMDAFLRDFG VEFASHYQGL RHDSGDPVEW GEKAIAHYEK
     LGIDPMTKTL VFSDNLDLQK AVELYRHFAS RVQLSFGIGT RLTCDIPQVK PLNIVIKLVE
     CNGKPVAKLS DSPGKTICHD KAFVRALRKA FDLPQVRKAS