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Protein

Nicotinate-nucleotide pyrophosphorylase [carboxylating]

Gene

QPRT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the catabolism of quinolinic acid (QA).1 Publication

Catalytic activityi

Beta-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.

Activity regulationi

Activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner.1 Publication

Kineticsi

  1. KM=21 µM for QA (at 0.1 mM PRPP)1 Publication
  2. KM=23 µM for QA (at 0.3 mM PRPP)1 Publication
  1. Vmax=1.2 µM/min/mg enzyme (at 0.3 mM QA and 0.1 mM PRPP)1 Publication
  2. Vmax=0.93 µM/min/mg enzyme (at 0.3 mM QA and 0.3 mM PRPP)1 Publication

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinate D-ribonucleotide from quinolinate.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinate-nucleotide pyrophosphorylase [carboxylating] (QPRT), Nicotinate-nucleotide pyrophosphorylase [carboxylating] (HEL-S-90n), Nicotinate-nucleotide pyrophosphorylase [carboxylating] (nadC), Nicotinate-nucleotide pyrophosphorylase [carboxylating] (nadC)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes nicotinate D-ribonucleotide from quinolinate, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei102Substrate1
Binding sitei161Substrate1
Binding sitei171Substrate1
Binding sitei201SubstrateBy similarity1
Binding sitei222SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processPyridine nucleotide biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02508-MONOMER
BRENDAi2.4.2.19 2681
ReactomeiR-HSA-196807 Nicotinate metabolism
UniPathwayi
UPA00253;UER00331

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC:2.4.2.19)
Alternative name(s):
Quinolinate phosphoribosyltransferase [decarboxylating]
Short name:
QAPRTase
Short name:
QPRTase
Gene namesi
Name:QPRT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000103485.17
HGNCiHGNC:9755 QPRT
MIMi606248 gene
neXtProtiNX_Q15274

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi102R → A or Q: Reduced activity. 1 Publication1
Mutagenesisi138R → Q: Loss of activity. 1 Publication1
Mutagenesisi139K → A or S: Loss of activity. 1 Publication1
Mutagenesisi161R → A: Reduced activity. 1 Publication1
Mutagenesisi161R → Q: Loss of activity. 1 Publication1
Mutagenesisi171K → A or S: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi23475
OpenTargetsiENSG00000103485
PharmGKBiPA34096

Chemistry databases

DrugBankiDB00627 Niacin

Polymorphism and mutation databases

BioMutaiQPRT
DMDMi296439291

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001559541 – 297Nicotinate-nucleotide pyrophosphorylase [carboxylating]Add BLAST297

Proteomic databases

EPDiQ15274
MaxQBiQ15274
PaxDbiQ15274
PeptideAtlasiQ15274
PRIDEiQ15274
ProteomicsDBi60508

PTM databases

iPTMnetiQ15274
PhosphoSitePlusiQ15274

Expressioni

Gene expression databases

BgeeiENSG00000103485 Expressed in 197 organ(s), highest expression level in cortex of kidney
CleanExiHS_QPRT
ExpressionAtlasiQ15274 baseline and differential
GenevisibleiQ15274 HS

Organism-specific databases

HPAiHPA011887

Interactioni

Subunit structurei

Hexamer formed by 3 homodimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NLGN3Q9NZ94-24EBI-739851,EBI-16423037

GO - Molecular functioni

Protein-protein interaction databases

BioGridi117035, 51 interactors
IntActiQ15274, 9 interactors
STRINGi9606.ENSP00000378782

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ15274
SMRiQ15274
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15274

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni137 – 139Substrate binding3
Regioni248 – 250Substrate bindingBy similarity3
Regioni269 – 271Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the NadC/ModD family.Curated

Phylogenomic databases

eggNOGiKOG3008 Eukaryota
COG0157 LUCA
GeneTreeiENSGT00390000002761
HOGENOMiHOG000224023
HOVERGENiHBG031727
InParanoidiQ15274
KOiK00767
OMAiVIMLDNM
OrthoDBiEOG091G10SF
PhylomeDBiQ15274
TreeFamiTF300845

Family and domain databases

CDDicd01572 QPRTase, 1 hit
Gene3Di3.20.20.70, 1 hit
3.90.1170.20, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR004393 NadC
IPR027277 NadC/ModD
IPR036068 Nicotinate_pribotase_like_C
IPR037128 Quinolinate_PRibosylTase_N_sf
IPR002638 Quinolinate_PRibosylTrfase_C
IPR022412 Quinolinate_PRibosylTrfase_N
PANTHERiPTHR32179 PTHR32179, 1 hit
PfamiView protein in Pfam
PF01729 QRPTase_C, 1 hit
PF02749 QRPTase_N, 1 hit
PIRSFiPIRSF006250 NadC_ModD, 1 hit
SUPFAMiSSF51690 SSF51690, 1 hit
TIGRFAMsiTIGR00078 nadC, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

Q15274-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAALWAKS
60 70 80 90 100
PGVLAGQPFF DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHCLLLG
110 120 130 140 150
ERVALNTLAR CSGIASAAAA AVEAARGAGW TGHVAGTRKT TPGFRLVEKY
160 170 180 190 200
GLLVGGAASH RYDLGGLVMV KDNHVVAAGG VEKAVRAARQ AADFTLKVEV
210 220 230 240 250
ECSSLQEAVQ AAEAGADLVL LDNFKPEELH PTATVLKAQF PSVAVEASGG
260 270 280 290
ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEV APVPKIH
Length:297
Mass (Da):30,846
Last modified:May 18, 2010 - v3
Checksum:iE3199814DB9FA0D5
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BP73H3BP73_HUMAN
Nicotinate-nucleotide pyrophosphory...
QPRT
149Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53V → I in AAP35895 (Ref. 2) Curated1
Sequence conflicti53V → I in AAH05060 (PubMed:15489334).Curated1
Sequence conflicti170V → L in BAA11242 (PubMed:9473669).Curated1
Sequence conflicti177 – 178AA → PP in BAA11242 (PubMed:9473669).Curated2
Sequence conflicti208A → V in BAA11242 (PubMed:9473669).Curated1
Sequence conflicti235V → A in BAA11242 (PubMed:9473669).Curated1
Sequence conflicti276A → V in BAA11242 (PubMed:9473669).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021915158A → V. Corresponds to variant dbSNP:rs2303255Ensembl.1
Natural variantiVAR_050219195T → ACombined sources3 PublicationsCorresponds to variant dbSNP:rs9932770Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78177 mRNA Translation: BAA11242.1
BT007231 mRNA Translation: AAP35895.1
BC005060 mRNA Translation: AAH05060.1
BC010033 mRNA Translation: AAH10033.1
BC018910 mRNA Translation: AAH18910.1
CCDSiCCDS10651.1
PIRiT46864
RefSeqiNP_001305178.1, NM_001318249.1
NP_001305179.1, NM_001318250.1
NP_055113.2, NM_014298.4
UniGeneiHs.513484
Hs.592544
Hs.675754

Genome annotation databases

EnsembliENST00000395384; ENSP00000378782; ENSG00000103485
GeneIDi23475
KEGGihsa:23475
UCSCiuc002dto.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78177 mRNA Translation: BAA11242.1
BT007231 mRNA Translation: AAP35895.1
BC005060 mRNA Translation: AAH05060.1
BC010033 mRNA Translation: AAH10033.1
BC018910 mRNA Translation: AAH18910.1
CCDSiCCDS10651.1
PIRiT46864
RefSeqiNP_001305178.1, NM_001318249.1
NP_001305179.1, NM_001318250.1
NP_055113.2, NM_014298.4
UniGeneiHs.513484
Hs.592544
Hs.675754

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JBMX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-297[»]
4KWVX-ray2.80A/B/C/D/E/F1-297[»]
4KWWX-ray2.55A/B/C/D/E/F1-297[»]
5AYXX-ray2.80A/B/C/D/E/F1-297[»]
5AYYX-ray3.09A/B/C/D/E/F/G/H/I1-297[»]
5AYZX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-297[»]
ProteinModelPortaliQ15274
SMRiQ15274
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117035, 51 interactors
IntActiQ15274, 9 interactors
STRINGi9606.ENSP00000378782

Chemistry databases

DrugBankiDB00627 Niacin

PTM databases

iPTMnetiQ15274
PhosphoSitePlusiQ15274

Polymorphism and mutation databases

BioMutaiQPRT
DMDMi296439291

Proteomic databases

EPDiQ15274
MaxQBiQ15274
PaxDbiQ15274
PeptideAtlasiQ15274
PRIDEiQ15274
ProteomicsDBi60508

Protocols and materials databases

DNASUi23475
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395384; ENSP00000378782; ENSG00000103485
GeneIDi23475
KEGGihsa:23475
UCSCiuc002dto.4 human

Organism-specific databases

CTDi23475
DisGeNETi23475
EuPathDBiHostDB:ENSG00000103485.17
GeneCardsiQPRT
HGNCiHGNC:9755 QPRT
HPAiHPA011887
MIMi606248 gene
neXtProtiNX_Q15274
OpenTargetsiENSG00000103485
PharmGKBiPA34096
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3008 Eukaryota
COG0157 LUCA
GeneTreeiENSGT00390000002761
HOGENOMiHOG000224023
HOVERGENiHBG031727
InParanoidiQ15274
KOiK00767
OMAiVIMLDNM
OrthoDBiEOG091G10SF
PhylomeDBiQ15274
TreeFamiTF300845

Enzyme and pathway databases

UniPathwayi
UPA00253;UER00331

BioCyciMetaCyc:HS02508-MONOMER
BRENDAi2.4.2.19 2681
ReactomeiR-HSA-196807 Nicotinate metabolism

Miscellaneous databases

EvolutionaryTraceiQ15274
GenomeRNAii23475
PROiPR:Q15274
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103485 Expressed in 197 organ(s), highest expression level in cortex of kidney
CleanExiHS_QPRT
ExpressionAtlasiQ15274 baseline and differential
GenevisibleiQ15274 HS

Family and domain databases

CDDicd01572 QPRTase, 1 hit
Gene3Di3.20.20.70, 1 hit
3.90.1170.20, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR004393 NadC
IPR027277 NadC/ModD
IPR036068 Nicotinate_pribotase_like_C
IPR037128 Quinolinate_PRibosylTase_N_sf
IPR002638 Quinolinate_PRibosylTrfase_C
IPR022412 Quinolinate_PRibosylTrfase_N
PANTHERiPTHR32179 PTHR32179, 1 hit
PfamiView protein in Pfam
PF01729 QRPTase_C, 1 hit
PF02749 QRPTase_N, 1 hit
PIRSFiPIRSF006250 NadC_ModD, 1 hit
SUPFAMiSSF51690 SSF51690, 1 hit
TIGRFAMsiTIGR00078 nadC, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNADC_HUMAN
AccessioniPrimary (citable) accession number: Q15274
Secondary accession number(s): Q53XW7, Q96G22, Q9BSG6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: September 12, 2018
This is version 170 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health

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