PNCB_ECO45
ID PNCB_ECO45 Reviewed; 400 AA.
AC B7MHP0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, 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=ECS88_0959;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928161; CAR02291.1; -; Genomic_DNA.
DR RefSeq; WP_001298298.1; NC_011742.1.
DR AlphaFoldDB; B7MHP0; -.
DR SMR; B7MHP0; -.
DR EnsemblBacteria; CAR02291; CAR02291; ECS88_0959.
DR KEGG; ecz:ECS88_0959; -.
DR HOGENOM; CLU_030991_1_0_6; -.
DR OMA; QAVFHRY; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000000747; 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..400
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_1000129465"
FT MOD_RES 220
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ SEQUENCE 400 AA; 45924 MW; 1A76FC61E75AE1D9 CRC64;
MTQFASPVLH SLLDTDAYKL HMQQAVFHHY YDVHVAAEFR CRGDDLLGIY ADAIREQVQA
MQHLRLQDDE YQWLSALPFF KADYLNWLRE FRFNPEQVTV SNDNGKLDIR LSGPWREVIL
WEVPLLAVIS EMVHRYRSPQ ADVAQALDTL ENKLVDFSAL TAGLDMSRFH LMDFGTRRRF
SREVQETIVK RLQQESWFVG TSNYDLARRL SLTPMGTQAH EWFQAHQQIS PDLANSQRAA
LAAWLEEYPD QLGIALTDCI TMDAFLRDFG VEFASRYQGL RHDSGDPVEW GEKAIAHYEK
LGIDPQSKTL VFSDNLDLRK AVELYRHFSS RVQLSFGIGT RLTCDIPQVK PLNIVIKLVE
CNGKPVAKLS DSPGKTICHD KAFVRALRKA FDLPHIKKAS