ID   PNCB_ACIAD              Reviewed;         407 AA.
AC   Q6F6W1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00570, ECO:0000303|PubMed:20926389};
DE            Short=NAPRTase {ECO:0000255|HAMAP-Rule:MF_00570};
DE            EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570, ECO:0000269|PubMed:20926389};
GN   Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570,
GN   ECO:0000303|PubMed:20926389}; OrderedLocusNames=ACIAD3562;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=20926389; DOI=10.1074/jbc.m110.185629;
RA   Sorci L., Blaby I., De Ingeniis J., Gerdes S., Raffaelli N.,
RA   de Crecy Lagard V., Osterman A.;
RT   "Genomics-driven reconstruction of acinetobacter NAD metabolism: insights
RT   for antibacterial target selection.";
RL   J. Biol. Chem. 285:39490-39499(2010).
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 (PubMed:20926389). Functions in the deamidating salvage pathway for
CC       production of NAD from nicotinamide (PubMed:20926389). Displays a
CC       strict preference for nicotinate over nicotinamide substrate
CC       (PubMed:20926389). {ECO:0000269|PubMed:20926389}.
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, ECO:0000269|PubMed:20926389};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36164;
CC         Evidence={ECO:0000269|PubMed:20926389};
CC   -!- ACTIVITY REGULATION: 100-fold more active in the presence of saturating
CC       ATP. {ECO:0000269|PubMed:20926389}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 uM for nicotinate {ECO:0000269|PubMed:20926389};
CC         KM=6900 uM for nicotinamide {ECO:0000269|PubMed:20926389};
CC         Note=kcat is 0.40 sec(-1) with nicotinate as substrate. kcat is 0.004
CC         sec(-1) with nicotinamide as substrate.
CC         {ECO:0000269|PubMed:20926389};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00570, ECO:0000269|PubMed:20926389}.
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   -!- DISRUPTION PHENOTYPE: The nadB-pncB double mutant loses the ability to
CC       grow on minimal medium supplemented by 0.1 mm nicotinate, but it can
CC       grow normally in the presence of 0.1 mm nicotinamide.
CC       {ECO:0000269|PubMed:20926389}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00570}.
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DR   EMBL; CR543861; CAG70204.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6F6W1; -.
DR   SMR; Q6F6W1; -.
DR   STRING; 202950.GCA_001485005_01652; -.
DR   KEGG; aci:ACIAD3562; -.
DR   eggNOG; COG1488; Bacteria.
DR   HOGENOM; CLU_030991_1_0_6; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01401; PncB_like; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 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   NCBIfam; TIGR01514; NAPRTase; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..407
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000205816"
FT   MOD_RES         228
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   407 AA;  47576 MW;  549EAC3E9EFB05F7 CRC64;
     MLSMSPIIHS LLDTDLYKFT MLQVVLHQFP QTHSVYHFRC RNLDETQYPL TDILDDLNEQ
     LDHLCTLKFK DDELQYLRSF RFIKSDFVDY LELFQLKRRF ITAGIDEEGR LDIWVEGPMV
     QAMMFEIFVL AIVNELYFRR IRSDAVLEEG ERRLQAKLAL LEQYQTQHQS DEPPFLVSDF
     GTRRRYSFEW QKHVIAAFHH HFPNIFRGTS NVLLAKELNI TPIGTMAHEF LQAFQALDVR
     LRDFQKAALE TWVQEYRGDL GIALTDVVGM DAFLRDFDLY FAKLFDGLRH DSGDPYEWGD
     KAYAHYRKLK IDTKTKMLTF SDGLNLEKAW ELHQYFKGRF KVSFGIGTNL TNDMGQTPLN
     IVLKLVECNG QSVAKISDSP GKTMTDNDTF LAYLRQVFQI AEEEPVA
//