Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
twitter

MetaCyc Enzyme: regulator of KefC-mediated potassium transport and quinone oxidoreductase

Gene: kefF Accession Numbers: EG11568 (MetaCyc), b0046, ECK0047

Synonyms: yabF

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of regulator of KefC-mediated potassium transport and quinone oxidoreductase = [KefF]2
         regulator of KefC-mediated potassium transport and quinone oxidoreductase = KefF

Summary:
KefF is an activator of potassium transport mediated by the KefC antiporter [Miller00b, Fujisawa07]. KefF also has enzymatic activity as a quinone oxidoreductase, thereby apparently reducing the redox toxicity of electrophilic quinones. This enzymatic activity of KefF is not required for its function as an activator of KefC [Lyngberg11]. NAD(P)H dehydrogenase activity of KefF was predicted based on sequence similarity [Reed03].

Crystal structures of an artificially constructed KefF fusion with the C-terminal domain of KefC have been solved [Roosild09, Roosild10]. KefF may exert its effect on the activity of KefC by influencing the angle of KefC's hinge domain [Roosild09].

A kefF mutant exhibits a defect in KefC-mediated potassium transport [Miller00b].

Expression in E. coli of a yabF gene of environmental origin results in carbonyl biosynthesis from polyols [Knietsch03].

Citations: [Miller97]

Locations: cytosol, inner membrane

Map Position: [47,246 -> 47,776]

Molecular Weight of Polypeptide: 20.17 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000159 , DIP:DIP-35822N , EchoBASE:EB1528 , EcoGene:EG11568 , EcoliWiki:b0046 , ModBase:P0A754 , OU-Microarray:b0046 , PortEco:kefF , PR:PRO_000023063 , Protein Model Portal:P0A754 , RefSeq:NP_414588 , RegulonDB:EG11568 , SMR:P0A754 , String:511145.b0046 , UniProt:P0A754

Relationship Links: InterPro:IN-FAMILY:IPR003680 , InterPro:IN-FAMILY:IPR023948 , PDB:Structure:3EYW , PDB:Structure:3L9W , PDB:Structure:3L9X , Pfam:IN-FAMILY:PF02525

Gene-Reaction Schematic: ?

Instance reaction of [a quinone + NAD(P)H + H+ → a quinol + NAD(P)+] (1.6.5.2):
i1: menadione + NADH + H+ = menadiol + NAD+ (1.6.99.5)

GO Terms:

Biological Process: GO:0032414 - positive regulation of ion transmembrane transporter activity Inferred from experiment Inferred by computational analysis [GOA06, Miller00b, Lyngberg11]
GO:0006813 - potassium ion transport Inferred by computational analysis [GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
GO:1901381 - positive regulation of potassium ion transmembrane transport Inferred by computational analysis [GOA06]
Molecular Function: GO:0003955 - NAD(P)H dehydrogenase (quinone) activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Lyngberg11]
GO:0009055 - electron carrier activity Inferred from experiment [Fujisawa07]
GO:0010181 - FMN binding Inferred from experiment Inferred by computational analysis [GOA06, Lyngberg11]
GO:0042803 - protein homodimerization activity Inferred from experiment [Lyngberg11]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: metabolism
regulation type of regulation posttranscriptional inhibition / activation of enzymes
transport

Credits:
Created in EcoCyc 11-Aug-2011 by Keseler I , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: quinone oxidoreductase

EC Number: 1.6.5.2

a quinone + NAD(P)H + H+ <=> a quinol + NAD(P)+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
Benzoquinone, menadione, and duroquinone as well as the 1-electron acceptors ferricyanide and DCIP can all serve as substrates. The enzyme utilizes both NADH and NADPH [Lyngberg11].

Cofactors or Prosthetic Groups: FMN [Lyngberg11]


Sequence Features

Feature Class Location Common Name Attached Group Citations Comment
Amino-Acid-Sites-That-Bind 8    
[UniProt13]
UniProt: FMN.
Nucleotide-Phosphate-Binding-Region 14 -> 17   FMN
[UniProt14]
UniProt: FMN.
Mutagenesis-Variant 41    
[UniProt13]
Alternate sequence: K; UniProt: Strongly reduced potassium efflux.
Nucleotide-Phosphate-Binding-Region 65 -> 68   FMN
[UniProt14]
UniProt: FMN.
Nucleotide-Phosphate-Binding-Region 105 -> 108   FMN
[UniProt14]
UniProt: FMN.
Mutagenesis-Variant 107    
[UniProt13]
Alternate sequence: S; UniProt: Does not bind FMN. Lacks oxidoreductase activity, but is still able to activate potassium efflux.
Mutagenesis-Variant 107 G107S mutant  
[Lyngberg11]
The G107S mutant does not bind FMN and has reduced enzymatic activity.
Mutagenesis-Variant 112    
[UniProt13]
Alternate sequence: W; UniProt: Lacks oxidoreductase activity, but is still able to activate potassium efflux.
Mutagenesis-Variant 149    
[UniProt13]
Alternate sequence: W; UniProt: Lacks oxidoreductase activity, but is still able to activate potassium efflux.

History:
10/20/97 Gene b0046 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11568; confirmed by SwissProt match.


References

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

Fujisawa07: Fujisawa M, Ito M, Krulwich TA (2007). "Three two-component transporters with channel-like properties have monovalent cation/proton antiport activity." Proc Natl Acad Sci U S A 104(33);13289-94. PMID: 17679694

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Knietsch03: Knietsch A, Waschkowitz T, Bowien S, Henne A, Daniel R (2003). "Construction and screening of metagenomic libraries derived from enrichment cultures: generation of a gene bank for genes conferring alcohol oxidoreductase activity on Escherichia coli." Appl Environ Microbiol 69(3);1408-16. PMID: 12620823

Lyngberg11: Lyngberg L, Healy J, Bartlett W, Miller S, Conway SJ, Booth IR, Rasmussen T (2011). "KefF, the regulatory subunit of the potassium efflux system KefC, shows quinone oxidoreductase activity." J Bacteriol 193(18);4925-32. PMID: 21742892

Miller00b: Miller S, Ness LS, Wood CM, Fox BC, Booth IR (2000). "Identification of an ancillary protein, YabF, required for activity of the KefC glutathione-gated potassium efflux system in Escherichia coli." J Bacteriol 182(22);6536-40. PMID: 11053405

Miller97: Miller S, Douglas RM, Carter P, Booth IR (1997). "Mutations in the glutathione-gated KefC K+ efflux system of Escherichia coli that cause constitutive activation." J Biol Chem 272(40);24942-7. PMID: 9312097

Reed03: Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)." Genome Biol 4(9);R54. PMID: 12952533

Roosild09: Roosild TP, Castronovo S, Miller S, Li C, Rasmussen T, Bartlett W, Gunasekera B, Choe S, Booth IR (2009). "KTN (RCK) domains regulate K+ channels and transporters by controlling the dimer-hinge conformation." Structure 17(6);893-903. PMID: 19523906

Roosild10: Roosild TP, Castronovo S, Healy J, Miller S, Pliotas C, Rasmussen T, Bartlett W, Conway SJ, Booth IR (2010). "Mechanism of ligand-gated potassium efflux in bacterial pathogens." Proc Natl Acad Sci U S A 107(46);19784-9. PMID: 21041667

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-01 released on 2014-01-01 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc13.