PNCB_CAEEL
ID PNCB_CAEEL Reviewed; 562 AA.
AC Q95XX1; Q8WTL1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000250|UniProtKB:P18133};
DE Short=NAPRTase {ECO:0000250|UniProtKB:P18133};
DE EC=6.3.4.21 {ECO:0000250|UniProtKB:P18133};
GN Name=nprt-1 {ECO:0000312|WormBase:Y54G2A.17b};
GN ORFNames=Y54G2A.17 {ECO:0000312|WormBase:Y54G2A.17b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC Helps prevent cellular oxidative stress via its role in NAD
CC biosynthesis. {ECO:0000250|UniProtKB:Q6XQN6}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q6XQN6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q6XQN6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q6XQN6};
CC Note=Activity is highest with Mn(2+). {ECO:0000250|UniProtKB:Q6XQN6};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000250|UniProtKB:Q6XQN6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:Y54G2A.17b};
CC IsoId=Q95XX1-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y54G2A.17a};
CC IsoId=Q95XX1-2; Sequence=VSP_030613;
CC Name=c {ECO:0000312|WormBase:Y54G2A.17c};
CC IsoId=Q95XX1-3; Sequence=VSP_030613, VSP_042230, VSP_042231;
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:0000250|UniProtKB:P22253}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
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DR EMBL; FO081809; CCD83505.1; -; Genomic_DNA.
DR EMBL; FO081809; CCD83544.1; -; Genomic_DNA.
DR EMBL; FO081809; CCD83545.1; -; Genomic_DNA.
DR RefSeq; NP_001023490.1; NM_001028319.3.
DR RefSeq; NP_500264.4; NM_067863.5.
DR RefSeq; NP_500265.3; NM_067864.4. [Q95XX1-1]
DR AlphaFoldDB; Q95XX1; -.
DR SMR; Q95XX1; -.
DR BioGRID; 42215; 4.
DR DIP; DIP-59878N; -.
DR IntAct; Q95XX1; 1.
DR STRING; 6239.Y54G2A.17b; -.
DR EPD; Q95XX1; -.
DR PaxDb; Q95XX1; -.
DR PeptideAtlas; Q95XX1; -.
DR EnsemblMetazoa; Y54G2A.17a.1; Y54G2A.17a.1; WBGene00021882. [Q95XX1-2]
DR EnsemblMetazoa; Y54G2A.17a.2; Y54G2A.17a.2; WBGene00021882. [Q95XX1-2]
DR EnsemblMetazoa; Y54G2A.17a.3; Y54G2A.17a.3; WBGene00021882. [Q95XX1-2]
DR EnsemblMetazoa; Y54G2A.17b.1; Y54G2A.17b.1; WBGene00021882. [Q95XX1-1]
DR EnsemblMetazoa; Y54G2A.17c.1; Y54G2A.17c.1; WBGene00021882. [Q95XX1-3]
DR GeneID; 177070; -.
DR KEGG; cel:CELE_Y54G2A.17; -.
DR UCSC; Y54G2A.17a.1; c. elegans. [Q95XX1-1]
DR CTD; 177070; -.
DR WormBase; Y54G2A.17a; CE46116; WBGene00021882; nprt-1. [Q95XX1-2]
DR WormBase; Y54G2A.17b; CE46281; WBGene00021882; nprt-1. [Q95XX1-1]
DR WormBase; Y54G2A.17c; CE33887; WBGene00021882; nprt-1. [Q95XX1-3]
DR eggNOG; KOG2511; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR InParanoid; Q95XX1; -.
DR OMA; VYFPGSP; -.
DR OrthoDB; 577034at2759; -.
DR PhylomeDB; Q95XX1; -.
DR Reactome; R-CEL-197264; Nicotinamide salvaging.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR UniPathway; UPA00253; UER00457.
DR PRO; PR:Q95XX1; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021882; Expressed in embryo and 4 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR041619; NAPRTase_C.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR11098; PTHR11098; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17956; NAPRTase_C; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR01513; NAPRTase_put; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Ligase; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..562
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000315685"
FT BINDING 36
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 183
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 225
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 397
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT MOD_RES 228
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P22253"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_030613"
FT VAR_SEQ 240..258
FT /note="LKVRLLNHKITNEKADLFQ -> VEHYLSIMGDFALNSSLWF (in
FT isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_042230"
FT VAR_SEQ 259..562
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_042231"
SQ SEQUENCE 562 AA; 63347 MW; C37B5385BC9EE745 CRC64;
MSFILPSESI DGTHPCNGLH MNGQDSLVQP LLTDFYQITM CYAYWKTGTH NEPAVFDVFF
RKNPFQGEFT VFAGLEDCLR FVENFKFSQS DIDYVKKILP ENAEPEFYEY LETLNGSHLT
IEAVAEGSVV FPKVPLLTIN GPLAMCQLIE TSILNLVNYA SLVATNAARF RQASGWKIQL
LEFGLRRAQG PNGGLTASKY CYIGGFDATS NVLAGKLYGI PVKGTQAHSF ICSFSSPAEL
KVRLLNHKIT NEKADLFQIS MEKRAWLLDQ FSWKAALSEV SDGELSAFVA YAIAFPDTFL
ALIDTYDVIR SGVVNFVAVS LALHDLGYRS MGCRIDSGDL SYLSKELREC FVKVSTLKGE
YKFFEKMSIV ASNDINEETI MSLNDQQHEI NAFGVGTHLV TCQKQPALGC VYKLVAQSAQ
PKIKLSQDVT KITIPGKKKC YRIFGKNGYA ILDLMMLEDE PEPQPNQQIL CRHPFEESKR
ALVNANKIIK LHNVYWKDGE MITPLPTLNE IKEHVNESIR STLRQDHRRY LNPTPYKVSV
SERLYQFLHT LWLQNAPIGQ LE
