ID DPYD_RAT Reviewed; 1025 AA. AC O89000; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 04-NOV-2008, entry version 53. DE RecName: Full=Dihydropyrimidine dehydrogenase [NADP+]; DE Short=DHPDHase; DE Short=DPD; DE EC=1.3.1.2; DE AltName: Full=Dihydrouracil dehydrogenase; DE AltName: Full=Dihydrothymine dehydrogenase; GN Name=Dpyd; Synonyms=DPD; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Liver; RX MEDLINE=99037149; PubMed=9819714; RA Kimura M., Fujimoto Sakata S., Matoba Y., Matsuda K., Kontani Y., RA Kaneko M., Tamaki N.; RT "Cloning of rat dihydropyrimidine dehydrogenase and correlation of its RT mRNA increase in the rat liver with age."; RL J. Nutr. Sci. Vitaminol. 44:537-546(1998). CC -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the CC reduction of uracil and thymine (By similarity). CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil + NADP(+) = uracil + NADPH. CC -!- COFACTOR: Binds 2 4Fe-4S clusters (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- ENZYME REGULATION: Inactivated by 5-iodouracil (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family. CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. 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; D85035; BAA33218.1; -; mRNA. DR RefSeq; NP_112289.1; -. DR UniGene; Rn.158382; -. DR HSSP; Q28943; 1H7X. DR SMR; O89000; 2-1017. DR Ensembl; ENSRNOG00000017105; Rattus norvegicus. DR GeneID; 81656; -. DR KEGG; rno:81656; -. DR RGD; 621218; Dpyd. DR HOVERGEN; O89000; -. DR NextBio; 615210; -. DR ArrayExpress; O89000; -. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) act...; IDA:UniProtKB. DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006214; P:thymidine catabolic process; ISS:UniProtKB. DR GO; GO:0006212; P:uracil catabolic process; ISS:UniProtKB. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd. DR InterPro; IPR000759; Adrndx_reductase. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; DHO_DHase_1_core. DR InterPro; IPR001295; Dihydroorotate_DHase_core. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR012285; Fum_reductase_C. DR InterPro; IPR016040; NAD(P)-bd. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01180; DHO_dh; 1. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00353; 4FE4SFRDOXIN. DR PRINTS; PR00419; ADXRDTASE. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00469; PNDRDTASEII. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 2: Evidence at transcript level; KW 4Fe-4S; Cytoplasm; FAD; Flavoprotein; FMN; Iron; Iron-sulfur; KW Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Repeat. FT CHAIN 1 1025 Dihydropyrimidine dehydrogenase [NADP+]. FT /FTId=PRO_0000327502. FT DOMAIN 69 100 4Fe-4S ferredoxin-type 1. FT DOMAIN 944 976 4Fe-4S ferredoxin-type 2. FT DOMAIN 978 1007 4Fe-4S ferredoxin-type 3. FT METAL 953 953 Iron-sulfur 1 (4Fe-4S) (Potential). FT METAL 956 956 Iron-sulfur 1 (4Fe-4S) (Potential). FT METAL 959 959 Iron-sulfur 1 (4Fe-4S) (Potential). FT METAL 963 963 Iron-sulfur 1 (4Fe-4S) (Potential). FT METAL 986 986 Iron-sulfur 2 (4Fe-4S) (Potential). FT METAL 989 989 Iron-sulfur 2 (4Fe-4S) (Potential). FT METAL 992 992 Iron-sulfur 2 (4Fe-4S) (Potential). FT METAL 996 996 Iron-sulfur 2 (4Fe-4S) (Potential). FT MOD_RES 577 577 Phosphoserine (By similarity). SQ SEQUENCE 1025 AA; 111468 MW; 07859E73D249828C CRC64; MAGVLSRDAP DIESILALNP RIQAHATLRS TMAKKLDKKH WKRNTDKNCF ICEKLENNFD DIKHTTLGER GALREAVRCL KCADAPCQKS CPTSLDIKSF ITSIANKNYY GAAKLIFSDN PLGLTCGMVC PTSDLCVGGC NLHATEEGPI NIGGLQQFAT EVFKAMNIPQ IRSPLLPPPE HMPEAYSAKI ALFGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV VNFEIELMKD LGVKIICGKS ISTDEMTLST LKENGYKAAF IGIGLPEPKK DHIFQGLTQV QGFYTSKDFL PLVAKGSKPG MCACHSPLPS VRGAVIVLGA GDTAFDCATS ALRCGARRVF IVFRKGFANI RAVPEEMELA KEEKCEFLPF LSPRKVIVKD GKIVGMQFVR TEQDETGNWV EDEEQIVRLK ADVVISPFGS VLDDPKVIEA LSPIKFNRWG LPEVNPETMQ TSEPWVFAGG DVVGMANTTV ESVNDGKQAS WYIHEYIQAQ YGALVPSQPT LPLFYTPVDL VDISVEMAGL RFPNPFGLAS ATPATSTPMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPLY GPGQSSFLNI ELISEKTAAY WCHSVTELKA DFPDNILIAS IMCSYNKNDW MELSKMAEAS GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ SVRVPFFAKL TPNVTDIVSI ARAAKEGGAD GVTATNTVSG LMGLKADGSP WPSVGSGKRT TYGGVSGTTI RPIALRAVTA IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL KSIEELSDWD GQSPPTMSHQ KGKPVPHIAE LMGQKLPSFG PYLERRKKIL AASKIRENDQ NRACSPLQRK HFNSQKPIPA IKDVIGKSLQ YLGTFGELNI MEQVVALIDE EMCINCGKCY MTCNDSGYQA IQFDPETHLP TVSDTCTGCT LCLSVCPIMD CIRMVSRATP YEPKRGLPLA VKPVC //