|Gene:||ynfF||Accession Numbers: G6846 (MetaCyc), b1588, ECK1583|
Species: Escherichia coli K-12 substr. MG1655
Component of: putative selenate reductase (summary available)
YnfF 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].
YnfF 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. When expressed together with DmsB and DmsC in a plasmid expression system, YnfF can form a complex with DmsB and DmsC, but the chimeric enzyme does not support growth on DMSO [Lubitz03].
The YnfF signal peptide can direct export through the twin arginine translocation (Tat) pathway and the general secretory pathway (Sec) pathway [TullmanErcek07].
YnfF is a predicted molybdoenzyme; deletion of ynfF does not confer a 6-N-hydroxylaminopurine (HAP)-sensitive phenotype [Kozmin07].
Locations: periplasmic space, inner membrane
|Map Position: [1,658,580 -> 1,661,003]|
Molecular Weight of Polypeptide: 89.987 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0005307 , DIP:DIP-12766N , EchoBASE:EB3605 , EcoGene:EG13844 , EcoliWiki:b1588 , ModBase:P77783 , OU-Microarray:b1588 , PortEco:ynfF , Pride:P77783 , Protein Model Portal:P77783 , RefSeq:NP_416105 , RegulonDB:G6846 , SMR:P77783 , String:511145.b1588 , UniProt:P77783
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 , InterPro:IN-FAMILY:IPR027467 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Prosite:IN-FAMILY:PS00551 , Prosite:IN-FAMILY:PS00932 , Prosite:IN-FAMILY:PS51318 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926
|Biological Process:||GO:0009061 - anaerobic respiration
GO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
|Molecular Function:||GO:0005515 - protein binding
GO:0033797 - selenate reductase activity [Guymer09]
GO:0003954 - NADH dehydrogenase activity [Gaudet10]
GO:0009055 - electron carrier activity [Gaudet10, GOA01a]
GO:0009389 - dimethyl sulfoxide reductase activity [GOA01a]
GO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01a]
GO:0030151 - molybdenum ion binding [Gaudet10, GOA01a]
GO:0046872 - metal ion binding [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding [UniProtGOA11a, Gaudet10]
GO:0051539 - 4 iron, 4 sulfur cluster binding [UniProtGOA11a, GOA01a]
|Cellular Component:||GO:0005886 - plasma membrane
GO:0016020 - membrane [UniProtGOA11a]
GO:0030288 - outer membrane-bounded periplasmic space [Gaudet10, 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.
|Feature Class||Location||Common Name||Citations||Comment|
|Signal-Sequence||1 -> 45||signal peptide|
|Chain||46 -> 807|
|Conserved-Region||52 -> 113|
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
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
Kozmin07: Kozmin SG, Schaaper RM (2007). "Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function." Mutat Res 619(1-2);9-15. PMID: 17349664
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
Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293
TullmanErcek07: Tullman-Ercek D, DeLisa MP, Kawarasaki Y, Iranpour P, Ribnicky B, Palmer T, Georgiou G (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282(11);8309-16. PMID: 17218314
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