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MetaCyc Polypeptide: oxidoreductase, predicted membrane anchor subunit

Gene: ynfH Accession Numbers: G6848 (MetaCyc), b1590, ECK1585

Species: Escherichia coli K-12 substr. MG1655

Component of: putative selenate reductase (summary available)

Summary:
YnfH contains eight potential transmembrane helices and is similar to DmsC, the membrane anchor subunit of the dimethyl sulfoxide reductase heterotrimer. When expressed together with DmsA and either DmsB or YnfG in a plasmid expression system, YnfH can form a complex with DmsA and DmsB/YnfG and support growth on DMSO [Lubitz03].

Locations: inner membrane

Map Position: [1,661,633 -> 1,662,487]

Molecular Weight of Polypeptide: 30.524 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0005311 , EchoBASE:EB3607 , EcoGene:EG13846 , EcoliWiki:b1590 , OU-Microarray:b1590 , PortEco:ynfH , Protein Model Portal:P76173 , RefSeq:NP_416107 , RegulonDB:G6848 , String:511145.b1590 , UniProt:P76173

Relationship Links: InterPro:IN-FAMILY:IPR007059 , Pfam:IN-FAMILY:PF04976

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0019645 - anaerobic electron transport chain Inferred by computational analysis [GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0009055 - electron carrier activity
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: metabolism metabolism of other compounds

Credits:
Imported from EcoCyc 16-Sep-2014 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: GO:0055114 - oxidation-reduction process Inferred from experiment [Lubitz03, Guymer09]
Molecular Function: GO:0033797 - selenate reductase activity Inferred from experiment [Guymer09]

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


Enzymatic reaction of: selenate reductase

EC Number: 1.97.1.9

selenate + a reduced electron acceptor <=> selenite + an oxidized electron acceptor + H2O

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.

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


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 10 -> 30
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 46 -> 66
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 87 -> 107
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 116 -> 136
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 149 -> 169
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 181 -> 201
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 223 -> 243
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 251 -> 271
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;

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


References

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

GOA01a: 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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 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 Thu Dec 18, 2014, BIOCYC14A.