DB code: D00048

CATH domain 3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.6.5.5
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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 1 D00001 D00002 D00018 D00481 D00482 D00490 D00492 D00615

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P28304 Quinone oxidoreductase
EC 1.6.5.5
NADPH:quinone reductase
Zeta-crystallin homolog protein
NP_418475.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492194.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]
Q8L3C8
Probable quinone oxidoreductase
EC 1.6.5.5
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical View]

KEGG enzyme name
NADPH:quinone reductase
NADPH2:quinone reductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P28304 QOR_ECOLI NADPH + 2 quinone = NADP(+) + 2 semiquinone. Homodimer.
Q8L3C8 Q8L3C8_THETH

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00005 C00472 C00006 C05309
E.C.
Compound NADPH Quinone NADP+ Semiquinone
Type amide group,amine group,nucleotide aromatic ring (only carbon atom) amide group,amine group,nucleotide aromatic ring (only carbon atom)
ChEBI 16474
 16474
 		16509
 16509
 		18009
 18009
PubChem 5884
 5884
 		4650
 4650
 		5886
 5886
1qorA01 Unbound Unbound Unbound Unbound
1qorB01 Unbound Unbound Unbound Unbound
1iyzA01 Unbound Unbound Unbound Unbound
1iz0A01 Unbound Unbound Unbound Unbound
1qorA02 Unbound Unbound Bound:NAP Unbound
1qorB02 Unbound Unbound Bound:NAP Unbound
1iyzA02 Bound:NDP Unbound Unbound Unbound
1iz0A02 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [8]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1qorA01 ASN 41;TYR 52
1qorB01 ASN 41;TYR 52
1iyzA01 ASN 38;TYR 49
1iz0A01 ASN 38;TYR 49
1qorA02 THR 127
1qorB02 THR 127
1iyzA02 THR 113
1iz0A02 THR 113

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 1370456
Journal J Biol Chem
Year 1992
Volume 267
Pages 96-102
Authors Rao PV, Krishna CM, Zigler JS Jr
Title Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8046753
Journal J Mol Biol
Year 1994
Volume 240
Pages 501-3
Authors Edwards KJ, Thorn JM, Daniher JA, Dixon NE, Ollis DL
Title Crystallization and preliminary X-ray diffraction studies on a soluble Escherichia coli quinone oxidoreductase.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 95326140
PubMed ID 7602590
Journal J Mol Biol
Year 1995
Volume 249
Pages 785-99
Authors Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ
Title Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.
Related PDB 1qor
Related UniProtKB P28304
[4]
Resource
Comments
Medline ID
PubMed ID 8638928
Journal Arch Biochem Biophys
Year 1996
Volume 328
Pages 173-83
Authors Edwards KJ, Barton JD, Rossjohn J, Thorn JM, Taylor GL, Ollis DL
Title Structural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8804573
Journal J Protein Chem
Year 1996
Volume 15
Pages 261-4
Authors Duhaiman AS
Title Inhibition of zeta-crystallin by Coumarins: a structure-activity study.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9774726
Journal Biochim Biophys Acta
Year 1998
Volume 1388
Pages 175-80
Authors Rabbani N, Duhaiman AS
Title Inhibition of camel lens zeta-crystallin/NADPH:quinone oxidoreductase by pyridoxal-5'-phosphate.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12199705
Journal Eur J Biochem
Year 2002
Volume 269
Pages 4267-76
Authors Nordling E, Jornvall H, Persson B
Title Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12837796
Journal J Bacteriol
Year 2003
Volume 185
Pages 4211-8
Authors Shimomura Y, Kakuta Y, Fukuyama K
Title Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition.
Related PDB 1iyz 1iz0
Related UniProtKB

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.

Created Updated
2004-10-25 2009-03-30