ID   PNCB_NEIG1              Reviewed;         402 AA.
AC   Q5F836;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 104.
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=NGO0962;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW89651.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE004969; AAW89651.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010358295.1; NC_002946.2.
DR   AlphaFoldDB; Q5F836; -.
DR   SMR; Q5F836; -.
DR   STRING; 242231.NGO_0962; -.
DR   EnsemblBacteria; AAW89651; AAW89651; NGO_0962.
DR   GeneID; 66753285; -.
DR   KEGG; ngo:NGO_0962; -.
DR   HOGENOM; CLU_030991_1_0_4; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000000535; 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..402
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000205832"
FT   MOD_RES         224
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   402 AA;  46265 MW;  87785B369B2D9AA0 CRC64;
     MTGIIHSLLD TDLYKFTMLQ VVLHQFPQTH SLYEFRCRNV STVYPLADIR EDLEAELDAL
     CRLRFTHDEL GYLRSLRFIK SDFVDYLELF QLQRRFVEVG TDDKGRLNIR IEGPMIQAMF
     FEIFILAIVN ELYFRRLETP AVIEEGERRL QAKAARLKEI AAAQNPDEPP FLISDFGTRR
     RYKLAWQEHV IRTLLEAAPS IVRGTSNVYL AKKLGITPIG TMAHEFLQAF QALDVRLRNF
     QKAALESWVH EYRGDLGVAL TDVVGMDAFL RDFDLYFAKL FDGLRHDSGD PYVWGDKAYA
     HYQKLKIDSR TKMLTFSDGL DIERSWALHQ YFKGRFKTGF GIGTNLTNDM GHTPLNIVLK
     LVECNGQSVA KLSDSPGKTM TNNSTFLAYL RQVFGIPEPR TP