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Protein

Dihydropteridine reductase

Gene

Qdpr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: Ensembl
  4. neuron projection Source: RGD
Complete GO annotation...

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 – 135Combined sources
Turni14 – 163Combined sources
Helixi18 – 2811Combined sources
Turni29 – 313Combined sources
Beta strandi33 – 408Combined sources
Beta strandi45 – 506Combined sources
Helixi57 – 7216Combined sources
Beta strandi77 – 826Combined sources
Helixi97 – 12226Combined sources
Beta strandi123 – 13210Combined sources
Helixi135 – 1384Combined sources
Helixi145 – 16117Combined sources
Beta strandi173 – 1808Combined sources
Helixi185 – 1906Combined sources
Helixi196 – 1983Combined sources
Beta strandi199 – 2013Combined sources
Helixi202 – 21312Combined sources
Turni214 – 2174Combined sources
Beta strandi224 – 2307Combined sources
Beta strandi233 – 2397Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiNRKSMPD.
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

        10         20         30         40         50
MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVI
60 70 80 90 100
VKMTDSFTEQ ADQVTAEVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN
110 120 130 140 150
CDLMWKQSIW TSTISSHLAT KHLKEGGLLT LAGAKAALDG TPGMIGYGMA
160 170 180 190 200
KGAVHQLCQS LAGKNSGMPS GAAAIAVLPV TLDTPMNRKS MPEADFSSWT
210 220 230 240
PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY F
Length:241
Mass (Da):25,552
Last modified:July 1, 1989 - v1
Checksum:iD9F7A5163E4B86EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
J03481 mRNA. Translation: AAA41099.1.
BC072536 mRNA. Translation: AAH72536.1.
PIRiA28473. RDRTP.
RefSeqiNP_071785.1. NM_022390.1.
UniGeneiRn.241.

3D structure databases

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

Protein-protein interaction databases

MINTiMINT-4565433.
STRINGi10116.ENSRNOP00000004385.

Chemistry

BindingDBiP11348.
ChEMBLiCHEMBL2910.

PTM databases

PhosphoSiteiP11348.

Proteomic databases

PaxDbiP11348.
PRIDEiP11348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5860.
RGDi619915. Qdpr.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_204731. Phenylalanine and tyrosine catabolism.
SABIO-RKP11348.

Miscellaneous databases

EvolutionaryTraceiP11348.
NextBioi612856.
PROiP11348.

Gene expression databases

GenevestigatoriP11348.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 121 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

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.