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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)DescriptionActionsGraphical viewLength
Active sitei147Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 35NADPAdd BLAST25

GO - Molecular functioni

  • 6,7-dihydropteridine reductase activity Source: UniProtKB
  • NADH binding Source: RGD
  • NADPH binding Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • cellular response to drug Source: RGD
  • liver development Source: RGD
  • L-phenylalanine catabolic process Source: RGD
  • response to aluminum ion Source: RGD
  • response to glucagon Source: RGD
  • response to lead ion Source: RGD
  • tetrahydrobiopterin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-RNO-71182. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi619915. Qdpr.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • mitochondrion Source: Ensembl
  • neuron projection Source: RGD
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000546391 – 241Dihydropteridine reductaseAdd BLAST241

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei70N6-succinyllysineBy similarity1
Modified residuei76N6-succinyllysineBy similarity1
Modified residuei93N6-succinyllysineBy similarity1
Modified residuei99N6-succinyllysineBy similarity1
Modified residuei170PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP11348.
PRIDEiP11348.

PTM databases

iPTMnetiP11348.
PhosphoSitePlusiP11348.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003253.
GenevisibleiP11348. RN.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

MINTiMINT-4565433.
STRINGi10116.ENSRNOP00000004385.

Chemistry databases

BindingDBiP11348.

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Turni14 – 16Combined sources3
Helixi18 – 28Combined sources11
Turni29 – 31Combined sources3
Beta strandi33 – 40Combined sources8
Beta strandi45 – 50Combined sources6
Helixi57 – 72Combined sources16
Beta strandi77 – 82Combined sources6
Helixi97 – 122Combined sources26
Beta strandi123 – 132Combined sources10
Helixi135 – 138Combined sources4
Helixi145 – 161Combined sources17
Beta strandi173 – 180Combined sources8
Helixi185 – 190Combined sources6
Helixi196 – 198Combined sources3
Beta strandi199 – 201Combined sources3
Helixi202 – 213Combined sources12
Turni214 – 217Combined sources4
Beta strandi224 – 230Combined sources7
Beta strandi233 – 239Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11348.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4022. Eukaryota.
ENOG4111D6J. LUCA.
GeneTreeiENSGT00390000000470.
HOGENOMiHOG000232194.
HOVERGENiHBG001000.
InParanoidiP11348.
KOiK00357.
OMAiNRKSMPD.
OrthoDBiEOG091G0ILG.
PhylomeDBiP11348.
TreeFamiTF105932.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DHRX-ray2.30A1-241[»]
1DIRX-ray2.60A/B/C/D1-241[»]
ProteinModelPortaliP11348.
SMRiP11348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4565433.
STRINGi10116.ENSRNOP00000004385.

Chemistry databases

BindingDBiP11348.
ChEMBLiCHEMBL2910.

PTM databases

iPTMnetiP11348.
PhosphoSitePlusiP11348.

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

eggNOGiKOG4022. Eukaryota.
ENOG4111D6J. LUCA.
GeneTreeiENSGT00390000000470.
HOGENOMiHOG000232194.
HOVERGENiHBG001000.
InParanoidiP11348.
KOiK00357.
OMAiNRKSMPD.
OrthoDBiEOG091G0ILG.
PhylomeDBiP11348.
TreeFamiTF105932.

Enzyme and pathway databases

ReactomeiR-RNO-71182. Phenylalanine and tyrosine catabolism.
SABIO-RKP11348.

Miscellaneous databases

EvolutionaryTraceiP11348.
PROiP11348.

Gene expression databases

BgeeiENSRNOG00000003253.
GenevisibleiP11348. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 134 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

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 one 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.