Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: disulfide reductase / organic hydroperoxide reductase



Gene: yghU Accession Numbers: G7553 (EcoCyc), b2989, ECK2983

Synonyms: GST N2-2

Regulation Summary Diagram: ?

Subunit composition of disulfide reductase / organic hydroperoxide reductase = [YghU]2
         disulfide reductase / organic hydroperoxide reductase = YghU

Summary:
YghU is one of eight glutathione transferase homologs in E. coli [Rife03]. YghU has modest activity with some organic hydroperoxides; the physiological substrates remain to be discovered [Stourman11].

Although yghU is located close to gss, there is no indication that YghU regulates gluthationylspermidine synthetase activity [Stourman11] as initially proposed [Rife03].

A crystal structure of YghU has been solved at 1.5 Å resolution. The structure reveals two molecules of glutathione bound in the active site [Stourman11].

Locations: cytosol

Map Position: [3,136,749 -> 3,137,615] (67.61 centisomes)
Length: 867 bp / 288 aa

Molecular Weight of Polypeptide: 32.392 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009812 , DIP:DIP-12212N , EchoBASE:EB2827 , EcoGene:EG13005 , EcoliWiki:b2989 , ModBase:Q46845 , OU-Microarray:b2989 , PortEco:yghU , Pride:Q46845 , Protein Model Portal:Q46845 , RefSeq:NP_417463 , RegulonDB:G7553 , SMR:Q46845 , String:511145.b2989 , UniProt:Q46845

Relationship Links: InterPro:IN-FAMILY:IPR004045 , InterPro:IN-FAMILY:IPR010987 , InterPro:IN-FAMILY:IPR012336 , InterPro:IN-FAMILY:IPR017933 , PDB:Structure:3C8E , Pfam:IN-FAMILY:PF00043 , Pfam:IN-FAMILY:PF13409 , Prosite:IN-FAMILY:PS50404 , Prosite:IN-FAMILY:PS50405

In Paralogous Gene Group: 210 (5 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0015036 - disulfide oxidoreductase activity Inferred from experiment [Stourman11]
GO:0042803 - protein homodimerization activity Inferred from experiment [Stourman11]
GO:0004601 - peroxidase activity Inferred by computational analysis [UniProtGOA11]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism central intermediary metabolism unassigned reversible reactions

Essentiality data for yghU knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Created 19-Jan-2011 by Keseler I , SRI International
Last-Curated ? 19-Jan-2011 by Keseler I , SRI International


Enzymatic reaction of: 2-hydroxyethyldisulfide reductase (disulfide reductase / organic hydroperoxide reductase)

2-hydroxyethyldisulfide + 2 glutathione <=> 2 2-mercaptoethanol + glutathione disulfide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.

Note: The enzyme may catalyze this reaction in vitro, but this reaction is not considered to be physiologically relevant.


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 26
[UniProt13]
UniProt: Glutathione 2.
Conserved-Region 46 -> 133
[UniProt09]
UniProt: GST N-terminal;
Protein-Segment 52 -> 54
[UniProt11]
UniProt: Glutathione binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 87
[UniProt11]
UniProt: Glutathione.
Amino-Acid-Sites-That-Bind 101
[UniProt11]
UniProt: Glutathione; via amide nitrogen and carbonyl oxygen.
Protein-Segment 117 -> 118
[UniProt11]
UniProt: Glutathione binding; Sequence Annotation Type: region of interest.
Conserved-Region 139 -> 265
[UniProt09]
UniProt: GST C-terminal;
Amino-Acid-Sites-That-Bind 151
[UniProt11]
UniProt: Glutathione.
Amino-Acid-Sites-That-Bind 178
[UniProt13]
UniProt: Glutathione 2.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
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.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

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

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Rife03: Rife CL, Parsons JF, Xiao G, Gilliland GL, Armstrong RN (2003). "Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli." Proteins 53(4);777-82. PMID: 14635120

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

Stourman11: Stourman NV, Branch MC, Schaab MR, Harp JM, Ladner JE, Armstrong RN (2011). "Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli." Biochemistry 50(7);1274-81. PMID: 21222452

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

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

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

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc13.