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Protein

Nicotinate-nucleotide pyrophosphorylase [carboxylating]

Gene

QPRT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Enzyme 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)
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

  • nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • NAD biosynthetic process Source: GO_Central
  • NAD metabolic process Source: Reactome
  • protein oligomerization Source: UniProtKB
  • quinolinate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02508-MONOMER.
ZFISH:HS02508-MONOMER.
BRENDAi2.4.2.19. 2681.
ReactomeiR-HSA-196807. Nicotinate metabolism.
UniPathwayiUPA00253; 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

HGNCiHGNC:9755. QPRT.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

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.

PTM databases

iPTMnetiQ15274.
PhosphoSitePlusiQ15274.

Expressioni

Gene expression databases

BgeeiENSG00000103485.
CleanExiHS_QPRT.
ExpressionAtlasiQ15274. baseline and differential.
GenevisibleiQ15274. HS.

Organism-specific databases

HPAiHPA011887.

Interactioni

Subunit structurei

Hexamer formed by 3 homodimers.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi117035. 47 interactors.
IntActiQ15274. 6 interactors.
MINTiMINT-1446481.
STRINGi9606.ENSP00000378782.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Helixi12 – 26Combined sources15
Helixi34 – 37Combined sources4
Beta strandi41 – 48Combined sources8
Beta strandi50 – 53Combined sources4
Helixi57 – 66Combined sources10
Beta strandi70 – 75Combined sources6
Beta strandi83 – 93Combined sources11
Helixi94 – 127Combined sources34
Beta strandi132 – 135Combined sources4
Helixi145 – 154Combined sources10
Turni161 – 163Combined sources3
Beta strandi166 – 170Combined sources5
Helixi172 – 178Combined sources7
Helixi181 – 192Combined sources12
Turni193 – 195Combined sources3
Beta strandi198 – 204Combined sources7
Helixi205 – 213Combined sources9
Beta strandi217 – 223Combined sources7
Helixi226 – 239Combined sources14
Beta strandi243 – 250Combined sources8
Turni253 – 255Combined sources3
Helixi256 – 259Combined sources4
Beta strandi266 – 268Combined sources3
Helixi271 – 274Combined sources4
Beta strandi281 – 288Combined sources8

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...

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.
OMAiDMIMLKD.
OrthoDBiEOG091G10SF.
PhylomeDBiQ15274.
TreeFamiTF300845.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004393. NadC.
IPR027277. NadC/ModD.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PfamiPF01729. QRPTase_C. 1 hit.
PF02749. QRPTase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006250. NadC_ModD. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.
TIGRFAMsiTIGR00078. nadC. 1 hit.

Sequencei

Sequence statusi: Complete.

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

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 rs2303255dbSNPEnsembl.1
Natural variantiVAR_050219195T → A.Combined sources3 PublicationsCorresponds to variant rs9932770dbSNPEnsembl.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

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. 47 interactors.
IntActiQ15274. 6 interactors.
MINTiMINT-1446481.
STRINGi9606.ENSP00000378782.

Chemistry databases

DrugBankiDB00627. Niacin.

PTM databases

iPTMnetiQ15274.
PhosphoSitePlusiQ15274.

Polymorphism and mutation databases

BioMutaiQPRT.
DMDMi296439291.

Proteomic databases

EPDiQ15274.
MaxQBiQ15274.
PaxDbiQ15274.
PeptideAtlasiQ15274.
PRIDEiQ15274.

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.
GeneCardsiQPRT.
HGNCiHGNC:9755. QPRT.
HPAiHPA011887.
MIMi606248. gene.
neXtProtiNX_Q15274.
OpenTargetsiENSG00000103485.
PharmGKBiPA34096.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00253; UER00331.
BioCyciMetaCyc:HS02508-MONOMER.
ZFISH:HS02508-MONOMER.
BRENDAi2.4.2.19. 2681.
ReactomeiR-HSA-196807. Nicotinate metabolism.

Miscellaneous databases

EvolutionaryTraceiQ15274.
GenomeRNAii23475.
PROiQ15274.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103485.
CleanExiHS_QPRT.
ExpressionAtlasiQ15274. baseline and differential.
GenevisibleiQ15274. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004393. NadC.
IPR027277. NadC/ModD.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PfamiPF01729. QRPTase_C. 1 hit.
PF02749. QRPTase_N. 1 hit.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 158 of the entry and version 3 of the sequence. [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

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.