[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Liver; PubMed=3680258 [NCBI, ExPASy, EBI, Israel, Japan] Shahbaz M., Hoch J.A., Trach K.A., Hural J.A., Webber S., Whiteley J.M.; "Structural studies and isolation of cDNA clones providing the complete sequence of rat liver dihydropteridine reductase."; J. Biol. Chem. 262:16412-16416(1987).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Heart; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 10-16; 53-70; 77-93; 100-121; 125-135; 152-164 AND 218-241, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus; Lubec G., Chen W.-Q., Kang S.U.; Submitted (JUL-2007) to UniProtKB.
[4]	PROTEIN SEQUENCE OF 13-14; 105-128; 192-220 AND 236-241. TISSUE=Liver; DOI=10.1016/0006-291X(87)91393-3; PubMed=3566737 [NCBI, ExPASy, EBI, Israel, Japan] Webber S., Hural J., Whiteley J.M.; "Preliminary studies on the primary structure of rat liver dihydropteridine reductase."; Biochem. Biophys. Res. Commun. 143:582-586(1987).
[5]	MUTAGENESIS. DOI=10.1016/0003-9861(91)90412-C; PubMed=1898002 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Role of aspartate-37 in determining cofactor specificity and binding in rat liver dihydropteridine reductase."; Arch. Biochem. Biophys. 287:234-239(1991).
[6]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). PubMed=1631094 [NCBI, ExPASy, EBI, Israel, Japan] Varughese K.I., Skinner M.M., Whiteley J.M., Matthews D.A., Xuong N.H.; "Crystal structure of rat liver dihydropteridine reductase."; Proc. Natl. Acad. Sci. U.S.A. 89:6080-6084(1992).
[7]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 6-241. PubMed=8304094 [NCBI, ExPASy, EBI, Israel, Japan] Varughese K.I., Su Y., Skinner M.M., Xuong N.H., Matthews D.A., Whiteley J.M.; "Two crystal structures of rat liver dihydropteridine reductase."; Adv. Exp. Med. Biol. 338:123-126(1993).

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

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J03481; AAA41099.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC072536; AAH72536.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A28473; RDRTP.

NP_071785.1; -.

3D structure databases

PDB

1DHR; X-ray; 2.30 A; A=1-241.	[ExPASy / RCSB / EBI]
1DIR; X-ray; 2.60 A; A/B/C/D=1-241.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DHR; -.
1DIR; -.

ModBase

P11348.

Organism-specific databases

RGD

619915; Qdpr.

Gene expression databases

ArrayExpress

P11348; -.

GermOnline

ENSRNOG00000003253; Rattus norvegicus.

Ontologies

GO:0004155;	Molecular function: 6,7-dihydropteridine reductase activity (inferred from mutant phenotype from UniProtKB).
GO:0006729;	Biological process: tetrahydrobiopterin biosynthetic process (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PROSITE

PS00061; ADH_SHORT; 1.

BLOCKS

P11348.

Genome annotation databases

Ensembl

ENSRNOG00000003253; Rattus norvegicus. [Contig view]

GeneID

64192; -.

KEGG

rno:64192; -.

NMPDR

fig|10116.3.peg.10476; -.

Phylogenomic databases

HOVERGEN

P11348; -.

Other

P11348; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; NADP; Oxidoreductase; Tetrahydrobiopterin biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 241`	`240`	`Dihydropteridine reductase.`	`PRO_0000054639`
`NP_BIND`	`11 35`	`25`	`NADP.`
`ACT_SITE`	`147 147`		`Proton acceptor.`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`STRAND`	`9 13`	`5`
`TURN`	`14 16`	`3`
`HELIX`	`18 28`	`11`
`TURN`	`29 31`	`3`
`STRAND`	`33 40`	`8`
`STRAND`	`45 50`	`6`
`HELIX`	`57 72`	`16`
`STRAND`	`77 82`	`6`
`HELIX`	`97 122`	`26`
`STRAND`	`123 132`	`10`
`HELIX`	`135 138`	`4`
`HELIX`	`145 161`	`17`
`STRAND`	`173 180`	`8`
`HELIX`	`185 190`	`6`
`HELIX`	`196 198`	`3`
`STRAND`	`199 201`	`3`
`HELIX`	`202 213`	`12`
`TURN`	`214 217`	`4`
`STRAND`	`224 230`	`7`
`STRAND`	`233 239`	`7`

Sequence information

Length: 241 AA [This is the length of the unprocessed precursor]

Molecular weight: 25552 Da [This is the MW of the unprocessed precursor]

CRC64: D9F7A5163E4B86EF [This is a checksum on the sequence]

        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

P11348 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools