ID DHPR_PIG Reviewed; 243 AA. AC Q8MJ30; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Dihydropteridine reductase; DE EC=1.5.1.34; DE AltName: Full=HDHPR; DE AltName: Full=Quinoid dihydropteridine reductase; GN Name=QDPR; Synonyms=DHPR; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=22351655; PubMed=12464030; RX DOI=10.1046/j.1365-2052.2002.00938_6.x; RA Kim J.G., Nonneman D., Vallet J.L., Rohrer G.A., Christenson R.K.; RT "Linkage mapping of a single nucleotide polymorphism (SNP) in the RT porcine QDPR gene to chromosome 8."; RL Anim. Genet. 33:474-474(2002). CC -!- FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), CC is an essential cofactor for phenylalanine, tyrosine, and CC tryptophan hydroxylases (By similarity). CC -!- CATALYTIC ACTIVITY: A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a CC 6,7-dihydropteridine + NAD(P)H. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF526879; AAM91996.1; -; mRNA. DR RefSeq; NP_999508.1; -. DR UniGene; Ssc.17250; -. DR HSSP; P11348; 1DHR. DR SMR; Q8MJ30; 8-243. DR GeneID; 397619; -. DR KEGG; ssc:397619; -. DR HOVERGEN; Q8MJ30; -. DR BRENDA; 1.5.1.34; 249. DR GO; GO:0004155; F:6,7-dihydropteridine reductase activity; ISS:UniProtKB. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; ISS:UniProtKB. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00106; adh_short; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Acetylation; NADP; Oxidoreductase; Tetrahydrobiopterin biosynthesis. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 243 Dihydropteridine reductase. FT /FTId=PRO_0000054638. FT NP_BIND 13 37 NADP (By similarity). FT ACT_SITE 149 149 Proton acceptor (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 243 AA; 25758 MW; 53A6634FE7D015CC CRC64; MAAAAAGEAR RVLVYGGRGA LGSRCVQAFR ARNWWVASID VVENEEASAN VVVKMTDSFT EQADQVTAEV GKLLGTEKVD AILCVAGGWA GGNAKSKSLF KNCDLMWKQS MWTSTISSHL ATKHLKEGGL LTLAGAKAAL DGTPGMIGYG MAKGAVHQLC QSLAGKDSGM PSGAAAIAVL PVTLDTPLNR KSMPHADFSS WTPLEFLVET FHDWIIEKNR PSSGSLIQVV TTQGKTELTP AYF //