Reviewed, UniProtKB/Swiss-Prot P11348 (DHPR_RAT)

Names and origin

Protein names

Recommended name:
    Dihydropteridine reductase
    EC=1.5.1.34
Alternative name(s):
    HDHPR
    Quinoid dihydropteridine reductase

Gene names

Name:	Qdpr
Synonyms:	Dhpr

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrobiopterin biosynthetic process Ref.5 Inferred from mutant phenotype. Source: UniProtKB
Molecular function	6,7-dihydropteridine reductase activity Ref.5 Inferred from mutant phenotype. Source: UniProtKB binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 241

240

Dihydropteridine reductase

PRO_0000054639

Regions

Nucleotide binding

11 – 35

25

NADP

Sites

Active site

147

1

Proton acceptor

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Secondary structure

1

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241

Helix Strand Turn

Details...

Beta strand

9 – 13

5

Turn

14 – 16

3

Helix

18 – 28

11

Turn

29 – 31

3

Beta strand

33 – 40

8

Beta strand

45 – 50

6

Helix

57 – 72

16

Beta strand

77 – 82

6

Helix

97 – 122

26

Beta strand

123 – 132

10

Helix

135 – 138

4

Helix

145 – 161

17

Beta strand

173 – 180

8

Helix

185 – 190

6

Helix

196 – 198

3

Beta strand

199 – 201

3

Helix

202 – 213

12

Turn

214 – 217

4

Beta strand

224 – 230

7

Beta strand

233 – 239

7

Sequences

	Sequence		Length	Mass (Da)
	P11348-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: D9F7A5163E4B86EF	FASTA	241	25,552
	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

References

	« Hide 'large scale' referencesShow '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: 3680258] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[3]	Lubec G., Chen W.-Q., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 10-16; 53-70; 77-93; 100-121; 125-135; 152-164 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: 3566737] [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: 1898002] [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: 1631094] [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: 8304094] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 6-241.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03481 mRNA. Translation: AAA41099.1.
BC072536 mRNA. Translation: AAH72536.1.

PIR

RDRTP. A28473.

RefSeq

NP_071785.1.

UniGene

Rn.241

3D structure databases

PDBMSD

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	[»]

ModBase

Search...

PTM databases

PhosphoSite

P11348.

Genome annotation databases

Ensembl

ENSRNOG00000003253. Rattus norvegicus. [Contig view]

GeneID

64192.

KEGG

rno:64192.

NMPDR

fig|10116.3.peg.10476.

Organism-specific databases

RGD

619915. Qdpr.

Phylogenomic databases

HOVERGEN

P11348.

Gene expression databases

ArrayExpress

P11348.

GermOnline

ENSRNOG00000003253. Rattus norvegicus.

Family and domain databases

InterPro

IPR002198. DHase_sc/Rdtase_SDR.
IPR016040. NAD(P)-bd.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P11348.

NextBio

612856.

Entry information

Entry name

DHPR_RAT

Accession

Primary (citable) accession number: P11348

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)