ID NQO1_CAVPO Reviewed; 275 AA. AC Q8CHK7; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=NAD(P)H dehydrogenase [quinone] 1; DE EC=1.6.5.2; DE AltName: Full=Quinone reductase 1; DE AltName: Full=NAD(P)H:quinone oxidoreductase 1; DE Short=QR1; DE AltName: Full=DT-diaphorase; DE Short=DTD; DE AltName: Full=Azoreductase; DE AltName: Full=Phylloquinone reductase; DE AltName: Full=Menadione reductase; GN Name=NQO1; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Hartley; RA Itoh K., Takahashi Y., Kitagawa M., Kamataki T.; RT "Inhibition of the transcription of the guinea pig NAD(P)H: quinone RT oxidoreductase1 (NQO1) gene by specificity protein 1 (Sp1)."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The enzyme apparently serves as a quinone reductase in CC connection with conjugation reactions of hydroquinons involved in CC detoxification pathways as well as in biosynthetic processes such CC as the vitamin K-dependent gamma-carboxylation of glutamate CC residues in prothrombin synthesis (By similarity). CC -!- CATALYTIC ACTIVITY: NAD(P)H + a quinone = NAD(P)(+) + a CC hydroquinone. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) 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; AB055403; BAC53985.1; -; mRNA. DR HSSP; P15559; 1H69. DR SMR; Q8CHK7; 5-275. DR Ensembl; ENSCPOG00000012430; Cavia porcellus. DR HOVERGEN; Q8CHK7; -. DR OMA; Q8CHK7; ESIWDET. DR BRENDA; 1.6.5.2; 44. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR003680; Flavodoxin_fold. DR Pfam; PF02525; Flavodoxin_2; 1. PE 2: Evidence at transcript level; KW Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase. FT CHAIN 1 275 NAD(P)H dehydrogenase [quinone] 1. FT /FTId=PRO_0000071621. FT NP_BIND 19 20 FAD (By similarity). FT NP_BIND 105 108 FAD (By similarity). FT NP_BIND 149 152 FAD (By similarity). FT REGION 127 129 Substrate binding (By similarity). FT BINDING 13 13 FAD (By similarity). FT BINDING 68 68 FAD (By similarity). FT BINDING 157 157 FAD (By similarity). FT BINDING 202 202 FAD (By similarity). SQ SEQUENCE 275 AA; 31086 MW; 15C475E39A7176C0 CRC64; MAALRRALII LAHSEKTSFN YAMKEAAVEA LQRKGWEVAV SDLYAMKFDP IISRKDITGA LKDPENFQYP AESALAYKES RLSPDIVTEQ KKVEEADLLI FQFPLQWFGV PAILKGWFER VFTGGFAYTY AAMYDKGPFQ NKKAVLSITT GGSESMYSLK GIHGDMNIIL WPIQSGTLHF CGFQVLEPQL TYGIGHTPPD VRTEILAGWK KRLENIWDET PLYFAPSSLF DLNFQAGFLL KKEIEDEQKN NKYGLSVGHH LGKPIPTDNQ IKARK //