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P11348 (DHPR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropteridine reductase
EC=1.5.1.34
Alternative name(s):
HDHPR
Quinoid dihydropteridine reductase
Gene names
Name:Qdpr
Synonyms:Dhpr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homodimer.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Dihydropteridine reductase
PRO_0000054639

Regions

Nucleotide binding11 – 3525NADP

Sites

Active site1471Proton acceptor

Secondary structure

1 ................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11348 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: D9F7A5163E4B86EF

FASTA24125,552
        10         20         30         40         50         60 
MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVI VKMTDSFTEQ 

        70         80         90        100        110        120 
ADQVTAEVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN CDLMWKQSIW TSTISSHLAT 

       130        140        150        160        170        180 
KHLKEGGLLT LAGAKAALDG TPGMIGYGMA KGAVHQLCQS LAGKNSGMPS GAAAIAVLPV 

       190        200        210        220        230        240 
TLDTPMNRKS MPEADFSSWT PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY 


F

« Hide

References

« Hide 'large scale' references
[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, 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]"Crystal structure of rat liver dihydropteridine reductase."
Varughese K.I., Skinner M.M., Whiteley J.M., Matthews D.A., Xuong N.H.
Proc. Natl. Acad. Sci. U.S.A. 89:6080-6084(1992) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03481 mRNA. Translation: AAA41099.1.
BC072536 mRNA. Translation: AAH72536.1.
IPIIPI00193151.
PIRRDRTP. A28473.
RefSeqNP_071785.1. NM_022390.1.
UniGeneRn.241.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHRX-ray2.30A1-241[»]
1DIRX-ray2.60A/B/C/D1-241[»]
ProteinModelPortalP11348.
SMRP11348. Positions 6-241.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000004385.

PTM databases

PhosphoSiteP11348.

Proteomic databases

PaxDbP11348.
PRIDEP11348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004385; ENSRNOP00000004385; ENSRNOG00000003253.
GeneID64192.
KEGGrno:64192.

Organism-specific databases

CTD5860.
RGD619915. Qdpr.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00390000000470.
HOGENOMHOG000232194.
HOVERGENHBG001000.
InParanoidP11348.
KOK00357.
OMASDLMWKQ.
OrthoDBEOG4QFWF7.

Enzyme and pathway databases

SABIO-RKP11348.

Gene expression databases

GenevestigatorP11348.
GermOnlineENSRNOG00000003253. Rattus norvegicus.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP11348.
ChEMBLCHEMBL2910.
EvolutionaryTraceP11348.
NextBio612856.

Entry information

Entry nameDHPR_RAT
AccessionPrimary (citable) accession number: P11348
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents