EzCatDB: D00048
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DB codeD00048
CATH domainDomain 13.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann foldCatalytic domain
E.C.1.6.5.5

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1D00001,D00002,D00018,D00481,D00482,D00490,D00492,D00615

Enzyme Name
UniProtKBKEGG

P28304Q8L3C8
Protein nameQuinone oxidoreductase 1
NADPH:quinone reductase
NADPH2:quinone reductase
SynonymsEC 1.6.5.5
NADPH:quinone reductase 1
Zeta-crystallin homolog protein
Probable quinone oxidoreductase
EC 1.6.5.5
RefSeqNP_418475.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492194.1 (Protein)
NC_007779.1 (DNA/RNA sequence)

PfamPF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]


UniProtKB:Accession NumberP28304Q8L3C8
Entry nameQOR_ECOLIQ8L3C8_THETH
ActivityNADPH + 2 quinone = NADP(+) + 2 semiquinone.
SubunitHomodimer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00005C00472C00006C05309
CompoundNADPHQuinoneNADP+Semiquinone
Typeamide group,amine group,nucleotidearomatic ring (only carbon atom)amide group,amine group,nucleotidearomatic ring (only carbon atom)
ChEBI16474
16509
18009

PubChem5884
4650
5886

            
1qorA01UnboundUnboundUnboundUnbound
1qorB01UnboundUnboundUnboundUnbound
1iyzA01UnboundUnboundUnboundUnbound
1iz0A01UnboundUnboundUnboundUnbound
1qorA02UnboundUnboundBound:NAPUnbound
1qorB02UnboundUnboundBound:NAPUnbound
1iyzA02Bound:NDPUnboundUnboundUnbound
1iz0A02UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [8]
pdbCatalytic residues
         
1qorA01ASN 41;TYR 52
1qorB01ASN 41;TYR 52
1iyzA01ASN 38;TYR 49
1iz0A01ASN 38;TYR 49
1qorA02THR 127
1qorB02THR 127
1iyzA02THR 113
1iz0A02THR 113


references
[1]
PubMed ID1370456
JournalJ Biol Chem
Year1992
Volume267
Pages96-102
AuthorsRao PV, Krishna CM, Zigler JS Jr
TitleIdentification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase.
[2]
PubMed ID8046753
JournalJ Mol Biol
Year1994
Volume240
Pages501-3
AuthorsEdwards KJ, Thorn JM, Daniher JA, Dixon NE, Ollis DL
TitleCrystallization and preliminary X-ray diffraction studies on a soluble Escherichia coli quinone oxidoreductase.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID95326140
PubMed ID7602590
JournalJ Mol Biol
Year1995
Volume249
Pages785-99
AuthorsThorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ
TitleCrystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.
Related PDB1qor
Related UniProtKBP28304
[4]
PubMed ID8638928
JournalArch Biochem Biophys
Year1996
Volume328
Pages173-83
AuthorsEdwards KJ, Barton JD, Rossjohn J, Thorn JM, Taylor GL, Ollis DL
TitleStructural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases.
[5]
PubMed ID8804573
JournalJ Protein Chem
Year1996
Volume15
Pages261-4
AuthorsDuhaiman AS
TitleInhibition of zeta-crystallin by Coumarins: a structure-activity study.
[6]
PubMed ID9774726
JournalBiochim Biophys Acta
Year1998
Volume1388
Pages175-80
AuthorsRabbani N, Duhaiman AS
TitleInhibition of camel lens zeta-crystallin/NADPH:quinone oxidoreductase by pyridoxal-5'-phosphate.
[7]
PubMed ID12199705
JournalEur J Biochem
Year2002
Volume269
Pages4267-76
AuthorsNordling E, Jornvall H, Persson B
TitleMedium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling.
[8]
PubMed ID12837796
JournalJ Bacteriol
Year2003
Volume185
Pages4211-8
AuthorsShimomura Y, Kakuta Y, Fukuyama K
TitleCrystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition.
Related PDB1iyz,1iz0

comments
This enzyme belongs to medium-chain alcohol dehydrogenase family.
Although the other homologous enzymes utilize zinc ion, this enzyme does not possess metal ions (see [5], [7]).
Although the tertiary structure of this enzyme has been determined, the detailed catalytic mechanism has not been elucidated yet.

createdupdated
2004-10-252009-03-30
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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