|Gene:||ynfE||Accession Numbers: G6845 (MetaCyc), b1587, ECK1582|
Species: Escherichia coli K-12 substr. MG1655
Component of: putative selenate reductase (summary available)
YnfE has been implicated as a Tat-dependent selenate reductase enzyme in E. coli. A ynfEF double null mutant is unable to reduce selenate to elemental selenium [Guymer09]. The disruption is specific to the initial selenate reduction process since selenium production is restored when selenite is added to the growth medium [Guymer09]. Production of either YnfE or YnfF from a plasmid restored the ability of the E. coli ynfEF double mutant to reduce selenate to selenium in vivo [Guymer09].
YnfE is highly similar to DmsA, the catalytic subunit of the dimethyl sulfoxide reductase heterotrimer, and cross-reacts with an anti-DmsA antibody. The protein is poorly expressed. In a plasmid expression system, expression of YnfE appears to inhibit expression of YnfFGH [Lubitz03].
In a ΔtusA strain, expression of ynfE is decreased in mid-exponential phase and under aerobic conditions [Dahl13].
Locations: periplasmic space, inner membrane
|Map Position: [1,656,093 -> 1,658,519]|
Molecular Weight of Polypeptide: 89.78 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0005302 , DIP:DIP-12765N , EchoBASE:EB3604 , EcoGene:EG13843 , EcoliWiki:b1587 , ModBase:P77374 , OU-Microarray:b1587 , PortEco:ynfE , Pride:P77374 , Protein Model Portal:P77374 , RefSeq:NP_416104 , RegulonDB:G6845 , SMR:P77374 , String:511145.b1587 , UniProt:P77374
Relationship Links: InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR006655 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006963 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR011888 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Prosite:IN-FAMILY:PS00932 , Prosite:IN-FAMILY:PS51318 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926
|Biological Process:||GO:0045333 - cellular respiration
GO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
|Molecular Function:||GO:0005515 - protein binding
GO:0033797 - selenate reductase activity [Guymer09]
GO:0009055 - electron carrier activity [GOA01a]
GO:0009389 - dimethyl sulfoxide reductase activity [GOA01a]
GO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01a]
GO:0030151 - molybdenum ion binding [GOA01a]
GO:0046872 - metal ion binding [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding [UniProtGOA11a]
GO:0051539 - 4 iron, 4 sulfur cluster binding [UniProtGOA11a, GOA01a]
|Cellular Component:||GO:0005886 - plasma membrane
GO:0016020 - membrane [UniProtGOA11a, Gaudet10]
GO:0030288 - outer membrane-bounded periplasmic space [DiazMejia09]
|MultiFun Terms:||metabolism → metabolism of other compounds|
Subunit of: putative selenate reductase
Synonyms: YnfFGH, YnfEFGH
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of
putative selenate reductase = [YnfE][YnfF][YnfG][YnfH]
oxidoreductase subunit = YnfE (summary available)
oxidoreductase subunit = YnfF (extended summary available)
oxidoreductase, predicted Fe-S subunit = YnfG (summary available)
oxidoreductase, predicted membrane anchor subunit = YnfH (summary available)
On the basis of sequence similarity the ynfEFGH operon was predicted to encode an oxidoreductase complex closely related to DMSO reductase. A strain carrying a deletion of dmsABC and containing ynfFGH on a multicopy plasmid is able to grow poorly under anaerobic conditions utilizing dimethyl sulfoxide as a terminal oxidant [Lubitz03]. More recently, genetic analysis of E.coli ynfE and ynfF null mutants suggests these proteins are Tat-targeted selenate reductases [Guymer09]. E.coli ubiE and menA null mutants are unable to reduce selenate to elemental red selenium in vivo thus implicating menaquinone in the reductase activity [Guymer09].
|Biological Process:||GO:0055114 - oxidation-reduction process [Lubitz03, Guymer09]|
|Molecular Function:||GO:0033797 - selenate reductase activity [Guymer09]|
Enzymatic reaction of: selenate reductase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown.
|Signal-Sequence||1 -> 43|
|Chain||44 -> 808|
|Conserved-Region||49 -> 110|
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
Dahl13: Dahl JU, Radon C, Buhning M, Nimtz M, Leichert LI, Denis Y, Jourlin-Castelli C, Iobbi-Nivol C, Mejean V, Leimkuhler S (2013). "The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis." J Biol Chem 288(8);5426-42. PMID: 23281480
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
Guymer09: Guymer D, Maillard J, Sargent F (2009). "A genetic analysis of in vivo selenate reduction by Salmonella enterica serovar Typhimurium LT2 and Escherichia coli K12." Arch Microbiol 191(6);519-28. PMID: 19415239
Lubitz03: Lubitz SP, Weiner JH (2003). "The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC)." Arch Biochem Biophys 418(2);205-16. PMID: 14522592
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