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P11348

- DHPR_RAT

UniProt

P11348 - DHPR_RAT

Protein

Dihydropteridine reductase

Gene

Qdpr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.

    Catalytic activityi

    A 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei147 – 1471Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 3525NADPAdd
    BLAST

    GO - Molecular functioni

    1. 6,7-dihydropteridine reductase activity Source: UniProtKB
    2. NADH binding Source: RGD
    3. NADPH binding Source: RGD
    4. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. cellular response to drug Source: RGD
    2. liver development Source: RGD
    3. L-phenylalanine catabolic process Source: RGD
    4. response to aluminum ion Source: RGD
    5. response to glucagon Source: RGD
    6. response to lead ion Source: RGD
    7. tetrahydrobiopterin biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tetrahydrobiopterin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_204731. Phenylalanine and tyrosine catabolism.
    SABIO-RKP11348.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropteridine reductase (EC:1.5.1.34)
    Alternative name(s):
    HDHPR
    Quinoid dihydropteridine reductase
    Gene namesi
    Name:Qdpr
    Synonyms:Dhpr
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi619915. Qdpr.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. mitochondrion Source: Ensembl
    3. neuron projection Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 241241Dihydropteridine reductasePRO_0000054639Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-succinyllysineBy similarity
    Modified residuei76 – 761N6-succinyllysineBy similarity
    Modified residuei93 – 931N6-succinyllysineBy similarity
    Modified residuei99 – 991N6-succinyllysineBy similarity

    Proteomic databases

    PaxDbiP11348.
    PRIDEiP11348.

    PTM databases

    PhosphoSiteiP11348.

    Expressioni

    Gene expression databases

    GenevestigatoriP11348.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    MINTiMINT-4565433.
    STRINGi10116.ENSRNOP00000004385.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Turni14 – 163
    Helixi18 – 2811
    Turni29 – 313
    Beta strandi33 – 408
    Beta strandi45 – 506
    Helixi57 – 7216
    Beta strandi77 – 826
    Helixi97 – 12226
    Beta strandi123 – 13210
    Helixi135 – 1384
    Helixi145 – 16117
    Beta strandi173 – 1808
    Helixi185 – 1906
    Helixi196 – 1983
    Beta strandi199 – 2013
    Helixi202 – 21312
    Turni214 – 2174
    Beta strandi224 – 2307
    Beta strandi233 – 2397

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DHRX-ray2.30A1-241[»]
    1DIRX-ray2.60A/B/C/D1-241[»]
    ProteinModelPortaliP11348.
    SMRiP11348. Positions 6-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11348.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00390000000470.
    HOGENOMiHOG000232194.
    HOVERGENiHBG001000.
    InParanoidiP11348.
    KOiK00357.
    OMAiSDLMWKQ.
    OrthoDBiEOG7060RV.
    PhylomeDBiP11348.
    TreeFamiTF105932.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P11348-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVI    50
    VKMTDSFTEQ ADQVTAEVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN 100
    CDLMWKQSIW TSTISSHLAT KHLKEGGLLT LAGAKAALDG TPGMIGYGMA 150
    KGAVHQLCQS LAGKNSGMPS GAAAIAVLPV TLDTPMNRKS MPEADFSSWT 200
    PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY F 241
    Length:241
    Mass (Da):25,552
    Last modified:July 1, 1989 - v1
    Checksum:iD9F7A5163E4B86EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03481 mRNA. Translation: AAA41099.1.
    BC072536 mRNA. Translation: AAH72536.1.
    PIRiA28473. RDRTP.
    RefSeqiNP_071785.1. NM_022390.1.
    UniGeneiRn.241.

    Genome annotation databases

    EnsembliENSRNOT00000004385; ENSRNOP00000004385; ENSRNOG00000003253.
    GeneIDi64192.
    KEGGirno:64192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03481 mRNA. Translation: AAA41099.1 .
    BC072536 mRNA. Translation: AAH72536.1 .
    PIRi A28473. RDRTP.
    RefSeqi NP_071785.1. NM_022390.1.
    UniGenei Rn.241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DHR X-ray 2.30 A 1-241 [» ]
    1DIR X-ray 2.60 A/B/C/D 1-241 [» ]
    ProteinModelPortali P11348.
    SMRi P11348. Positions 6-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4565433.
    STRINGi 10116.ENSRNOP00000004385.

    Chemistry

    BindingDBi P11348.
    ChEMBLi CHEMBL2910.

    PTM databases

    PhosphoSitei P11348.

    Proteomic databases

    PaxDbi P11348.
    PRIDEi P11348.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000004385 ; ENSRNOP00000004385 ; ENSRNOG00000003253 .
    GeneIDi 64192.
    KEGGi rno:64192.

    Organism-specific databases

    CTDi 5860.
    RGDi 619915. Qdpr.

    Phylogenomic databases

    eggNOGi COG1028.
    GeneTreei ENSGT00390000000470.
    HOGENOMi HOG000232194.
    HOVERGENi HBG001000.
    InParanoidi P11348.
    KOi K00357.
    OMAi SDLMWKQ.
    OrthoDBi EOG7060RV.
    PhylomeDBi P11348.
    TreeFami TF105932.

    Enzyme and pathway databases

    Reactomei REACT_204731. Phenylalanine and tyrosine catabolism.
    SABIO-RK P11348.

    Miscellaneous databases

    EvolutionaryTracei P11348.
    NextBioi 612856.
    PROi P11348.

    Gene expression databases

    Genevestigatori P11348.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural studies and isolation of cDNA clones providing the complete sequence of rat liver dihydropteridine reductase."
      Shahbaz M., Hoch J.A., Trach K.A., Hural J.A., Webber S., Whiteley J.M.
      J. Biol. Chem. 262:16412-16416(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. "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].
      Tissue: Heart.
    3. Lubec G., Chen W.-Q., Kang S.U.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 10-16; 53-70; 77-93; 100-121; 125-164 AND 218-241, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.
    4. "Preliminary studies on the primary structure of rat liver dihydropteridine reductase."
      Webber S., Hural J., Whiteley J.M.
      Biochem. Biophys. Res. Commun. 143:582-586(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 13-14; 105-128; 192-220 AND 236-241.
      Tissue: Liver.
    5. "Role of aspartate-37 in determining cofactor specificity and binding in rat liver dihydropteridine reductase."
      Matthews D.A., Varughese K.I., Skinner M.M., Xuing N.H., Hoch J.A., Trach K.A., Schneider M., Bray T., Whiteley J.M.
      Arch. Biochem. Biophys. 287:234-239(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    7. "Two crystal structures of rat liver dihydropteridine reductase."
      Varughese K.I., Su Y., Skinner M.M., Xuong N.H., Matthews D.A., Whiteley J.M.
      Adv. Exp. Med. Biol. 338:123-126(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 6-241.

    Entry informationi

    Entry nameiDHPR_RAT
    AccessioniPrimary (citable) accession number: P11348
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3