PNCB_NEIG2
ID PNCB_NEIG2 Reviewed; 402 AA.
AC B4RL23;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=NGK_0833;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF29514.1; -; Genomic_DNA.
DR RefSeq; WP_010358295.1; NC_011035.1.
DR AlphaFoldDB; B4RL23; -.
DR SMR; B4RL23; -.
DR EnsemblBacteria; ACF29514; ACF29514; NGK_0833.
DR GeneID; 66753285; -.
DR KEGG; ngk:NGK_0833; -.
DR HOGENOM; CLU_030991_1_0_4; -.
DR OMA; VMGFEIF; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000002564; 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.
FT CHAIN 1..402
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_1000129475"
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