PNCB_EDWI9
ID PNCB_EDWI9 Reviewed; 401 AA.
AC C5BD56;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=NT01EI_1361;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR68551.1; -; Genomic_DNA.
DR RefSeq; WP_015870716.1; NC_012779.2.
DR AlphaFoldDB; C5BD56; -.
DR SMR; C5BD56; -.
DR STRING; 67780.B6E78_00165; -.
DR EnsemblBacteria; ACR68551; ACR68551; NT01EI_1361.
DR GeneID; 7960444; -.
DR KEGG; eic:NT01EI_1361; -.
DR PATRIC; fig|634503.3.peg.1224; -.
DR HOGENOM; CLU_030991_1_0_6; -.
DR OMA; QAVFHRY; -.
DR OrthoDB; 241792at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000001485; 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..401
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_1000212084"
FT MOD_RES 221
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ SEQUENCE 401 AA; 45538 MW; 6CC3CEA4DB8DE6DD CRC64;
MTQDVSPIIT SLLDTDAYKL HMQQAVYHRY RNVSVAAEFR CRGDELLGEY AGEIANQVNL
MGQLALTQDE YDYLAALPFF QRDYLDWLRT LRLDPRRVAI SNDRGRLNIR ISGPWREVIL
WEVPLLAVIS EVVHRHRSPH ITPEVAAAQL QRRLSEFRHL SADVDLRGFH LIDFGTRRRF
SRAVHQAILT TLKSEFPYLS GTSNYLFAKQ MALTPLGTQA HEWFQAHQQI CPVLANSQRA
ALQSWLDEYP DQLGIALTDC ITMDAFLRDF GSQFAGHYQG LRHDSGDPIA WGEKAIAHYE
QLGLDPQDKM LVFSDNLDLP KALALYRHFH HRINLSFGIG TRLTCDLPGV RPLNIVIKLV
ECNGKPVAKL SDSPGKTICQ DAAFVKALRK AFDLPLVKRA S