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P11348

- DHPR_RAT

UniProt

P11348 - DHPR_RAT

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Protein
Dihydropteridine reductase
Gene
Qdpr, Dhpr
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 – 3525NADP
Add
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
Complete GO annotation...

GO - Biological processi

  1. L-phenylalanine catabolic process Source: RGD
  2. cellular response to drug Source: RGD
  3. liver development 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. mitochondrion Source: Ensembl
  3. neuron projection Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Dihydropteridine reductase
PRO_0000054639Add
BLAST

Amino acid modifications

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

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.

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...

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

« 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: September 3, 2014
This is version 116 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

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