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Q15274

- NADC_HUMAN

UniProt

Q15274 - NADC_HUMAN

Protein

Nicotinate-nucleotide pyrophosphorylase [carboxylating]

Gene

QPRT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    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

    Vmax=1.2 µM/min/mg enzyme (at 0.3 mM QA and 0.1 mM PRPP)1 Publication

    Vmax=0.93 µM/min/mg enzyme (at 0.3 mM QA and 0.3 mM PRPP)1 Publication

    Pathwayi

    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

    1. nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. NAD biosynthetic process Source: UniProtKB-UniPathway
    2. NAD metabolic process Source: Reactome
    3. protein oligomerization Source: UniProtKB
    4. quinolinate catabolic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. vitamin metabolic process Source: Reactome
    7. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02508-MONOMER.
    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: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9755. QPRT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    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.

    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

    ArrayExpressiQ15274.
    BgeeiQ15274.
    CleanExiHS_QPRT.
    GenevestigatoriQ15274.

    Organism-specific databases

    HPAiHPA011887.

    Interactioni

    Subunit structurei

    Hexamer formed by 3 homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi117035. 4 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 – 97
    Helixi12 – 2615
    Helixi34 – 374
    Beta strandi41 – 488
    Helixi57 – 6610
    Beta strandi70 – 756
    Beta strandi83 – 9311
    Helixi94 – 12734
    Beta strandi132 – 1354
    Helixi145 – 15410
    Turni161 – 1633
    Beta strandi166 – 1705
    Helixi172 – 1787
    Helixi181 – 19212
    Turni193 – 1953
    Beta strandi198 – 2047
    Helixi205 – 2139
    Beta strandi217 – 2237
    Helixi226 – 23914
    Beta strandi243 – 2508
    Turni253 – 2553
    Helixi256 – 2594
    Beta strandi266 – 2683
    Helixi271 – 2744
    Beta strandi281 – 2888

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000224023.
    HOVERGENiHBG031727.
    InParanoidiQ15274.
    KOiK00767.
    OMAiFAIKVEV.
    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

    MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAALWAKS    50
    PGVLAGQPFF DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHCLLLG 100
    ERVALNTLAR CSGIASAAAA AVEAARGAGW TGHVAGTRKT TPGFRLVEKY 150
    GLLVGGAASH RYDLGGLVMV KDNHVVAAGG VEKAVRAARQ AADFTLKVEV 200
    ECSSLQEAVQ AAEAGADLVL LDNFKPEELH PTATVLKAQF PSVAVEASGG 250
    ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEV APVPKIH 297
    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. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi296439291.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10651.1.
    PIRi T46864.
    RefSeqi NP_055113.2. NM_014298.3.
    UniGenei Hs.513484.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JBM X-ray 2.00 A/B/C/D/E/F/G/H/I/J/K/L 1-297 [» ]
    3LAR X-ray 2.80 A/B/C/D/E/F 1-297 [» ]
    4KWV X-ray 2.80 A/B/C/D/E/F 1-297 [» ]
    4KWW X-ray 2.55 A/B/C/D/E/F 1-297 [» ]
    ProteinModelPortali Q15274.
    SMRi Q15274. Positions 1-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117035. 4 interactions.
    IntActi Q15274. 3 interactions.
    MINTi MINT-1446481.
    STRINGi 9606.ENSP00000378782.

    Chemistry

    DrugBanki DB00627. Niacin.

    PTM databases

    PhosphoSitei Q15274.

    Polymorphism databases

    DMDMi 296439291.

    Proteomic databases

    MaxQBi Q15274.
    PaxDbi Q15274.
    PRIDEi Q15274.

    Protocols and materials databases

    DNASUi 23475.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395384 ; ENSP00000378782 ; ENSG00000103485 .
    GeneIDi 23475.
    KEGGi hsa:23475.
    UCSCi uc002dto.3. human.

    Organism-specific databases

    CTDi 23475.
    GeneCardsi GC16P029690.
    HGNCi HGNC:9755. QPRT.
    HPAi HPA011887.
    MIMi 606248. gene.
    neXtProti NX_Q15274.
    PharmGKBi PA34096.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0157.
    HOGENOMi HOG000224023.
    HOVERGENi HBG031727.
    InParanoidi Q15274.
    KOi K00767.
    OMAi FAIKVEV.
    OrthoDBi EOG77Q4X9.
    PhylomeDBi Q15274.
    TreeFami TF300845.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00331 .
    BioCyci MetaCyc:HS02508-MONOMER.
    Reactomei REACT_11088. Nicotinate metabolism.

    Miscellaneous databases

    EvolutionaryTracei Q15274.
    GenomeRNAii 23475.
    NextBioi 45813.
    PROi Q15274.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15274.
    Bgeei Q15274.
    CleanExi HS_QPRT.
    Genevestigatori Q15274.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.90.1170.20. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR004393. NadC.
    IPR027277. NadC/ModD.
    IPR002638. Quinolinate_PRibosylTrfase_C.
    IPR022412. Quinolinate_PRibosylTrfase_N.
    [Graphical view ]
    Pfami PF01729. QRPTase_C. 1 hit.
    PF02749. QRPTase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006250. NadC_ModD. 1 hit.
    SUPFAMi SSF51690. SSF51690. 1 hit.
    TIGRFAMsi TIGR00078. nadC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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: October 1, 2014
    This is version 137 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