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MetaCyc Polypeptide: oxidoreductase subunit

Gene: ynfE Accession Numbers: G6845 (MetaCyc), b1587, ECK1582

Species: Escherichia coli K-12 substr. MG1655

Component of: putative selenate reductase (summary available)

Summary:
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 [Dahl13a].

Locations: periplasm, 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

Gene-Reaction Schematic

Gene-Reaction Schematic


GO Terms:
Biological Process:
Inferred by computational analysisGO:0009061 - anaerobic respiration [Gaudet10]
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11, GOA01]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Chan09]
Inferred from experimentGO:0033797 - selenate reductase activity [Guymer09]
Inferred by computational analysisGO:0003954 - NADH dehydrogenase activity [Gaudet10]
Inferred by computational analysisGO:0009055 - electron carrier activity [GOA01, Gaudet10]
Inferred by computational analysisGO:0009389 - dimethyl sulfoxide reductase activity [GOA01]
Inferred by computational analysisGO:0016491 - oxidoreductase activity [UniProtGOA11, GOA01]
Inferred by computational analysisGO:0030151 - molybdenum ion binding [GOA01, Gaudet10]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11]
Inferred by computational analysisGO:0051536 - iron-sulfur cluster binding [UniProtGOA11, Gaudet10]
Inferred by computational analysisGO:0051539 - 4 iron, 4 sulfur cluster binding [UniProtGOA11, GOA01]
Cellular Component:
Inferred by computational analysisGO:0005886 - plasma membrane [UniProtGOA11a, UniProtGOA11]
Inferred by computational analysisGO:0016020 - membrane [UniProtGOA11]
Inferred by computational analysisGO:0030288 - outer membrane-bounded periplasmic space [Gaudet10, DiazMejia09]

MultiFun Terms: metabolismmetabolism of other compounds

Credits:
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International


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)

Summary:
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].


GO Terms:
Biological Process:
Inferred from experimentGO:0055114 - oxidation-reduction process [Lubitz03, Guymer09]
Molecular Function:
Inferred from experimentGO:0033797 - selenate reductase activity [Guymer09]

Credits:
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International


Enzymatic reaction of: selenate reductase

Inferred from experiment

EC Number: 1.97.1.9

selenate + an reduced unknown electron acceptor → selenite + an oxidized unknown electron acceptor + H2O

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 43
Inferred by computational analysis[UniProt15]
UniProt: Tat-type signal.
Chain 44 -> 808
Author statement[UniProt15]
UniProt: Putative dimethyl sulfoxide reductase chain YnfE.
Conserved-Region 49 -> 110
Inferred by computational analysis[UniProt15]
UniProt: 4Fe-4S Mo/W bis-MGD-type.
Metal-Binding-Site 56
Inferred by computational analysis[UniProt15]
UniProt: Iron-sulfur (4Fe-4S).
Metal-Binding-Site 60
Inferred by computational analysis[UniProt15]
UniProt: Iron-sulfur (4Fe-4S).
Metal-Binding-Site 64
Inferred by computational analysis[UniProt15]
UniProt: Iron-sulfur (4Fe-4S).
Metal-Binding-Site 96
Inferred by computational analysis[UniProt15]
UniProt: Iron-sulfur (4Fe-4S).
Metal-Binding-Site 196
Inferred by computational analysis[UniProt15]
UniProt: Molybdenum.

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Chan09: Chan CS, Chang L, Rommens KL, Turner RJ (2009). "Differential Interactions between Tat-specific redox enzyme peptides and their chaperones." J Bacteriol 191(7);2091-101. PMID: 19151138

Dahl13a: 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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

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

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

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms 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 Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc13.