[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=12464030 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.G., Nonneman D., Vallet J.L., Rohrer G.A., Christenson R.K.; "Linkage mapping of a single nucleotide polymorphism (SNP) in the porcine QDPR gene to chromosome 8."; Anim. Genet. 33:474-474(2002).

Comments

FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases (By similarity).
CATALYTIC ACTIVITY: A 5,6,7,8-tetrahydropteridine + NAD(P)⁺ = a 6,7-dihydropteridine + NAD(P)H.
SUBUNIT: Homodimer (By similarity).
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

AF526879; AAM91996.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_999508.1; -.

UniGene

Ssc.17250

3D structure databases

HSSP

P11348; 1DHR. [HSSP ENTRY / PDB]

SMR

Q8MJ30; 8-243.

ModBase

Q8MJ30.

Ontologies

GO:0004155;	Molecular function: 6,7-dihydropteridine reductase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006729;	Biological process: tetrahydrobiopterin biosynthetic process (inferred from sequence or structural similarity 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.

PROSITE

PS00061; ADH_SHORT; 1.

BLOCKS

Q8MJ30.

Genome annotation databases

GeneID

397619; -.

KEGG

ssc:397619; -.

Phylogenomic databases

HOVERGEN

Q8MJ30; -.

Other

ProtoNet

Q8MJ30.

UniRef

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

Keywords

Acetylation; NADP; Oxidoreductase; Tetrahydrobiopterin biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 243`	`242`	`Dihydropteridine reductase.`	`PRO_0000054638`
`NP_BIND`	`13 37`	`25`	`NADP (By similarity).`
`ACT_SITE`	`149 149`		`Proton acceptor (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`

Sequence information

Length: 243 AA [This is the length of the unprocessed precursor]

Molecular weight: 25758 Da [This is the MW of the unprocessed precursor]

CRC64: 53A6634FE7D015CC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAAAGEAR RVLVYGGRGA LGSRCVQAFR ARNWWVASID VVENEEASAN VVVKMTDSFT 

        70         80         90        100        110        120 
EQADQVTAEV GKLLGTEKVD AILCVAGGWA GGNAKSKSLF KNCDLMWKQS MWTSTISSHL 

       130        140        150        160        170        180 
ATKHLKEGGL LTLAGAKAAL DGTPGMIGYG MAKGAVHQLC QSLAGKDSGM PSGAAAIAVL 

       190        200        210        220        230        240 
PVTLDTPLNR KSMPHADFSS WTPLEFLVET FHDWIIEKNR PSSGSLIQVV TTQGKTELTP 


AYF

Q8MJ30 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