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Escherichia coli K-12 substr. MG1655 Enzyme: quinone oxidoreductase



Gene: qor Accession Numbers: EG11492 (EcoCyc), b4051, ECK4043

Synonyms: hzc, hcz

Regulation Summary Diagram: ?

Subunit composition of quinone oxidoreductase = [Qor]2

Locations: cytosol

Map Position: [4,261,271 <- 4,262,254] (91.84 centisomes)
Length: 984 bp / 327 aa

Molecular Weight of Polypeptide: 35.172 kD (from nucleotide sequence)

pI: 8.51

Unification Links: ASAP:ABE-0013262 , CGSC:36654 , DIP:DIP-10631N , EchoBASE:EB1455 , EcoGene:EG11492 , EcoliWiki:b4051 , Mint:MINT-1267314 , ModBase:P28304 , OU-Microarray:b4051 , PortEco:qor , Pride:P28304 , Protein Model Portal:P28304 , RefSeq:NP_418475 , RegulonDB:EG11492 , SMR:P28304 , String:511145.b4051 , UniProt:P28304

Relationship Links: InterPro:IN-FAMILY:IPR002085 , InterPro:IN-FAMILY:IPR002364 , InterPro:IN-FAMILY:IPR011032 , InterPro:IN-FAMILY:IPR013149 , InterPro:IN-FAMILY:IPR013154 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR11695 , PDB:Structure:1QOR , Pfam:IN-FAMILY:PF00107 , Pfam:IN-FAMILY:PF08240 , Prosite:IN-FAMILY:PS01162

In Paralogous Gene Group: 103 (13 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0003960 - NADPH:quinone reductase activity Inferred by computational analysis [GOA01a]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Edwards94]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism energy production/transport electron carriers

Essentiality data for qor knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Enzymatic reaction of: quinone oxidoreductase

EC Number: 1.6.5.5

a quinone + NADPH <=> a semiquinone + NADP+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Summary:
Quinone oxidoreductase catalyzes the reduction of a variety of simple quinones, in a NAD(P)H-dependent reaction. The enzyme shows a preference for NADPH over NADH. [Edwards94, Thorn95]

Inhibitors (Unknown Mechanism): dicoumarol [Thorn95]


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 42 -> 46
[UniProt10]
UniProt: NADP;
Amino-Acid-Sites-That-Bind 130
[UniProt10]
UniProt: NADP;
Nucleotide-Phosphate-Binding-Region 152 -> 153
[UniProt10]
UniProt: NADP;
Nucleotide-Phosphate-Binding-Region 173 -> 177
[UniProt10]
UniProt: NADP;
Amino-Acid-Sites-That-Bind 192
[UniProt10]
UniProt: NADP;
Amino-Acid-Sites-That-Bind 216
[UniProt10]
UniProt: NADP; via carbonyl oxygen;
Nucleotide-Phosphate-Binding-Region 238 -> 241
[UniProt10]
UniProt: NADP;
Nucleotide-Phosphate-Binding-Region 264 -> 266
[UniProt10]
UniProt: NADP;
Amino-Acid-Sites-That-Bind 317
[UniProt10]
UniProt: NADP;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b4051 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11492; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Edwards94: Edwards KJ, Thorn JM, Daniher JA, Dixon NE, Ollis DL (1994). "Crystallization and preliminary X-ray diffraction studies on a soluble Escherichia coli quinone oxidoreductase." J Mol Biol 1994;240(5);501-3. PMID: 8046753

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Thorn95: Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ (1995). "Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH." J Mol Biol 1995;249(4);785-99. PMID: 7602590

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, BIOCYC13A.