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Q15274 (NADC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinate-nucleotide pyrophosphorylase [carboxylating]

EC=2.4.2.19
Alternative name(s):
Quinolinate phosphoribosyltransferase [decarboxylating]
Short name=QAPRTase
Short name=QPRTase
Gene names
Name:QPRT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the catabolism of quinolinic acid (QA). Ref.4

Catalytic activity

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

Enzyme regulation

Activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner. Ref.4

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.

Subunit structure

Hexamer formed by 3 homodimers. Ref.4

Sequence similarities

Belongs to the NadC/ModD family.

Biophysicochemical properties

Kinetic parameters:

KM=21 µM for QA (at 0.1 mM PRPP) Ref.4

KM=23 µM for QA (at 0.3 mM PRPP)

Vmax=1.2 µM/min/mg enzyme (at 0.3 mM QA and 0.1 mM PRPP)

Vmax=0.93 µM/min/mg enzyme (at 0.3 mM QA and 0.3 mM PRPP)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Nicotinate-nucleotide pyrophosphorylase [carboxylating]
PRO_0000155954

Regions

Region137 – 1393Substrate binding
Region248 – 2503Substrate binding By similarity
Region269 – 2713Substrate binding By similarity

Sites

Binding site1021Substrate
Binding site1611Substrate
Binding site1711Substrate
Binding site2011Substrate By similarity
Binding site2221Substrate By similarity

Natural variations

Natural variant1581A → V.
Corresponds to variant rs2303255 [ dbSNP | Ensembl ].
VAR_021915
Natural variant1951T → A. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs9932770 [ dbSNP | Ensembl ].
VAR_050219

Experimental info

Mutagenesis1021R → A or Q: Reduced activity. Ref.4
Mutagenesis1381R → Q: Loss of activity. Ref.4
Mutagenesis1391K → A or S: Loss of activity. Ref.4
Mutagenesis1611R → A: Reduced activity. Ref.4
Mutagenesis1611R → Q: Loss of activity. Ref.4
Mutagenesis1711K → A or S: Loss of activity. Ref.4
Sequence conflict531V → I in AAP35895. Ref.2
Sequence conflict531V → I in AAH05060. Ref.3
Sequence conflict1701V → L in BAA11242. Ref.1
Sequence conflict177 – 1782AA → PP in BAA11242. Ref.1
Sequence conflict2081A → V in BAA11242. Ref.1
Sequence conflict2351V → A in BAA11242. Ref.1
Sequence conflict2761A → V in BAA11242. Ref.1

Secondary structure

............................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15274 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: E3199814DB9FA0D5

FASTA29730,846
        10         20         30         40         50         60 
MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAALWAKS PGVLAGQPFF 

        70         80         90        100        110        120 
DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHCLLLG ERVALNTLAR CSGIASAAAA 

       130        140        150        160        170        180 
AVEAARGAGW TGHVAGTRKT TPGFRLVEKY GLLVGGAASH RYDLGGLVMV KDNHVVAAGG 

       190        200        210        220        230        240 
VEKAVRAARQ AADFTLKVEV ECSSLQEAVQ AAEAGADLVL LDNFKPEELH PTATVLKAQF 

       250        260        270        280        290 
PSVAVEASGG ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEV APVPKIH 

« Hide

References

« Hide 'large scale' references
[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]"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.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10651.1.
PIRT46864.
RefSeqNP_055113.2. NM_014298.3.
UniGeneHs.513484.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ15274.
SMRQ15274. Positions 1-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117035. 4 interactions.
IntActQ15274. 3 interactions.
MINTMINT-1446481.
STRING9606.ENSP00000378782.

Chemistry

DrugBankDB00627. Niacin.

PTM databases

PhosphoSiteQ15274.

Polymorphism databases

DMDM296439291.

Proteomic databases

MaxQBQ15274.
PaxDbQ15274.
PRIDEQ15274.

Protocols and materials databases

DNASU23475.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395384; ENSP00000378782; ENSG00000103485.
GeneID23475.
KEGGhsa:23475.
UCSCuc002dto.3. human.

Organism-specific databases

CTD23475.
GeneCardsGC16P029690.
HGNCHGNC:9755. QPRT.
HPAHPA011887.
MIM606248. gene.
neXtProtNX_Q15274.
PharmGKBPA34096.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0157.
HOGENOMHOG000224023.
HOVERGENHBG031727.
InParanoidQ15274.
KOK00767.
OMAFAIKVEV.
OrthoDBEOG77Q4X9.
PhylomeDBQ15274.
TreeFamTF300845.

Enzyme and pathway databases

BioCycMetaCyc:HS02508-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00253; UER00331.

Gene expression databases

ArrayExpressQ15274.
BgeeQ15274.
CleanExHS_QPRT.
GenevestigatorQ15274.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR004393. NadC.
IPR027277. NadC/ModD.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PfamPF01729. QRPTase_C. 1 hit.
PF02749. QRPTase_N. 1 hit.
[Graphical view]
PIRSFPIRSF006250. NadC_ModD. 1 hit.
SUPFAMSSF51690. SSF51690. 1 hit.
TIGRFAMsTIGR00078. nadC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ15274.
GenomeRNAi23475.
NextBio45813.
PROQ15274.
SOURCESearch...

Entry information

Entry nameNADC_HUMAN
AccessionPrimary (citable) accession number: Q15274
Secondary accession number(s): Q53XW7, Q96G22, Q9BSG6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM