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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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei102 – 1021Substrate
Binding sitei161 – 1611Substrate
Binding sitei171 – 1711Substrate
Binding sitei201 – 2011SubstrateBy similarity
Binding sitei222 – 2221SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02508-MONOMER.
BRENDAi2.4.2.19. 2681.
ReactomeiREACT_11088. 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
ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi102 – 1021R → A or Q: Reduced activity. 1 Publication
Mutagenesisi138 – 1381R → Q: Loss of activity. 1 Publication
Mutagenesisi139 – 1391K → A or S: Loss of activity. 1 Publication
Mutagenesisi161 – 1611R → A: Reduced activity. 1 Publication
Mutagenesisi161 – 1611R → Q: Loss of activity. 1 Publication
Mutagenesisi171 – 1711K → A or S: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA34096.

Chemistry

DrugBankiDB00627. Niacin.

Polymorphism and mutation databases

BioMutaiQPRT.
DMDMi296439291.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Nicotinate-nucleotide pyrophosphorylase [carboxylating]PRO_0000155954Add
BLAST

Proteomic databases

MaxQBiQ15274.
PaxDbiQ15274.
PRIDEiQ15274.

PTM databases

PhosphoSiteiQ15274.

Expressioni

Gene expression databases

BgeeiQ15274.
CleanExiHS_QPRT.
ExpressionAtlasiQ15274. baseline and differential.
GenevisibleiQ15274. HS.

Organism-specific databases

HPAiHPA011887.

Interactioni

Subunit structurei

Hexamer formed by 3 homodimers.1 Publication

Protein-protein interaction databases

BioGridi117035. 43 interactions.
IntActiQ15274. 3 interactions.
MINTiMINT-1446481.
STRINGi9606.ENSP00000378782.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Helixi12 – 2615Combined sources
Helixi34 – 374Combined sources
Beta strandi41 – 488Combined sources
Helixi57 – 6610Combined sources
Beta strandi70 – 756Combined sources
Beta strandi83 – 9311Combined sources
Helixi94 – 12734Combined sources
Beta strandi132 – 1354Combined sources
Helixi145 – 15410Combined sources
Turni161 – 1633Combined sources
Beta strandi166 – 1705Combined sources
Helixi172 – 1787Combined sources
Helixi181 – 19212Combined sources
Turni193 – 1953Combined sources
Beta strandi198 – 2047Combined sources
Helixi205 – 2139Combined sources
Beta strandi217 – 2237Combined sources
Helixi226 – 23914Combined sources
Beta strandi243 – 2508Combined sources
Turni253 – 2553Combined sources
Helixi256 – 2594Combined sources
Beta strandi266 – 2683Combined sources
Helixi271 – 2744Combined sources
Beta strandi281 – 2888Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JBMX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-297[»]
3LARX-ray2.80A/B/C/D/E/F1-297[»]
4KWVX-ray2.80A/B/C/D/E/F1-297[»]
4KWWX-ray2.55A/B/C/D/E/F1-297[»]
ProteinModelPortaliQ15274.
SMRiQ15274. Positions 1-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15274.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 1393Substrate binding
Regioni248 – 2503Substrate bindingBy similarity
Regioni269 – 2713Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the NadC/ModD family.Curated

Phylogenomic databases

eggNOGiCOG0157.
GeneTreeiENSGT00390000002761.
HOGENOMiHOG000224023.
HOVERGENiHBG031727.
InParanoidiQ15274.
KOiK00767.
OMAiCGGCHNH.
OrthoDBiEOG77Q4X9.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531V → I in AAP35895 (Ref. 2) Curated
Sequence conflicti53 – 531V → I in AAH05060 (PubMed:15489334).Curated
Sequence conflicti170 – 1701V → L in BAA11242 (PubMed:9473669).Curated
Sequence conflicti177 – 1782AA → PP in BAA11242 (PubMed:9473669).Curated
Sequence conflicti208 – 2081A → V in BAA11242 (PubMed:9473669).Curated
Sequence conflicti235 – 2351V → A in BAA11242 (PubMed:9473669).Curated
Sequence conflicti276 – 2761A → V in BAA11242 (PubMed:9473669).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti158 – 1581A → V.
Corresponds to variant rs2303255 [ dbSNP | Ensembl ].
VAR_021915
Natural varianti195 – 1951T → A.4 Publications
Corresponds to variant rs9932770 [ dbSNP | Ensembl ].
VAR_050219

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_055113.2. NM_014298.3.
UniGeneiHs.513484.

Genome annotation databases

EnsembliENST00000395384; ENSP00000378782; ENSG00000103485.
GeneIDi23475.
KEGGihsa:23475.
UCSCiuc002dto.3. 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_055113.2. NM_014298.3.
UniGeneiHs.513484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JBMX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-297[»]
3LARX-ray2.80A/B/C/D/E/F1-297[»]
4KWVX-ray2.80A/B/C/D/E/F1-297[»]
4KWWX-ray2.55A/B/C/D/E/F1-297[»]
ProteinModelPortaliQ15274.
SMRiQ15274. Positions 1-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117035. 43 interactions.
IntActiQ15274. 3 interactions.
MINTiMINT-1446481.
STRINGi9606.ENSP00000378782.

Chemistry

DrugBankiDB00627. Niacin.

PTM databases

PhosphoSiteiQ15274.

Polymorphism and mutation databases

BioMutaiQPRT.
DMDMi296439291.

Proteomic databases

MaxQBiQ15274.
PaxDbiQ15274.
PRIDEiQ15274.

Protocols and materials databases

DNASUi23475.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395384; ENSP00000378782; ENSG00000103485.
GeneIDi23475.
KEGGihsa:23475.
UCSCiuc002dto.3. human.

Organism-specific databases

CTDi23475.
GeneCardsiGC16P029677.
HGNCiHGNC:9755. QPRT.
HPAiHPA011887.
MIMi606248. gene.
neXtProtiNX_Q15274.
PharmGKBiPA34096.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0157.
GeneTreeiENSGT00390000002761.
HOGENOMiHOG000224023.
HOVERGENiHBG031727.
InParanoidiQ15274.
KOiK00767.
OMAiCGGCHNH.
OrthoDBiEOG77Q4X9.
PhylomeDBiQ15274.
TreeFamiTF300845.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00331.
BioCyciMetaCyc:HS02508-MONOMER.
BRENDAi2.4.2.19. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.

Miscellaneous databases

EvolutionaryTraceiQ15274.
GenomeRNAii23475.
NextBioi45813.
PROiQ15274.
SOURCEiSearch...

Gene expression databases

BgeeiQ15274.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and functional expression of the cDNA encoding human brain quinolinate phosphoribosyltransferase."
    Fukuoka S., Nyaruhucha C.M., Shibata K.
    Biochim. Biophys. Acta 1395:192-201(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-195.
    Tissue: Brain.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-195.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-195.
    Tissue: Kidney, Muscle and Placenta.
  4. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens."
    Liu H., Woznica K., Catton G., Crawford A., Botting N., Naismith J.H.
    J. Mol. Biol. 373:755-763(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF ARG-102; ARG-138; LYS-139; ARG-161 AND LYS-171, FUNCTION, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 24, 2015
This is version 146 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

External Data

Dasty 3

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 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.