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Escherichia coli K-12 substr. MG1655 Enzyme: predicted oxidoreductase with NAD(P)-binding Rossmann-fold domain



Gene: yohF Accession Numbers: EG12019 (EcoCyc), b2137, ECK2130

Synonyms: yohE

Regulation Summary Diagram: ?

Summary:
Based on sequence similarity, YohF was predicted to be an acetoin dehydrogenase (diacetyl reductase) [Reed03].

An NADPH-dependent diacetyl reductase with a molecular weight of approximately 10 kDa was isolated from E. coli B [Silber74]. The gene encoding this enzyme was not identified, and no physiological role was proposed for it. The true acetoin reductases of the butanediol pathway in Enterobacter aerogenes and other organisms utilize NADH as the electron donor. It is now thought that the diacetyl reductase activity was due to a side activity of another dehydrogenase enzyme ([ECOSAL], Module 3.5.3).

Transcription of yohF is dependent on σS and is induced upon inhibition of acetolactate synthase activity by treatment with sulfometuron methyl, an herbicide [Van98].

Citations: [ParadisBleau14]

Locations: cytosol

Map Position: [2,224,531 <- 2,225,292] (47.95 centisomes)
Length: 762 bp / 253 aa

Molecular Weight of Polypeptide: 26.951 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0007062 , DIP:DIP-12806N , EchoBASE:EB1955 , EcoGene:EG12019 , EcoliWiki:b2137 , ModBase:P33368 , OU-Microarray:b2137 , PortEco:yohF , Pride:P33368 , Protein Model Portal:P33368 , RefSeq:NP_416641 , RegulonDB:EG12019 , SMR:P33368 , String:511145.b2137 , UniProt:P33368

Relationship Links: InterPro:IN-FAMILY:IPR002198 , InterPro:IN-FAMILY:IPR002347 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR020904 , Pfam:IN-FAMILY:PF00106 , Prints:IN-FAMILY:PR00080 , Prints:IN-FAMILY:PR00081 , Prosite:IN-FAMILY:PS00061

In Paralogous Gene Group: 272 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0019152 - acetoin dehydrogenase activity Inferred by computational analysis
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization

Essentiality data for yohF 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:
Last-Curated ? 24-Nov-2009 by Keseler I , SRI International


Enzymatic reaction of: predicted acetoin dehydrogenase (predicted oxidoreductase with NAD(P)-binding Rossmann-fold domain)

Synonyms: diacetyl reductase, acetoin:NAD+ oxidoreductase, acetoin dehydrogenase

EC Number: 1.1.1.-

acetoin + NADP+ <=> diacetyl + NADPH + H+

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.


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 6 -> 30
[UniProt10]
UniProt: NAD or NADP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 140
[UniProt10]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Active-Site 153
[UniProt10]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2137 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12019; confirmed by SwissProt match.


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

ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

ParadisBleau14: Paradis-Bleau C, Kritikos G, Orlova K, Typas A, Bernhardt TG (2014). "A genome-wide screen for bacterial envelope biogenesis mutants identifies a novel factor involved in cell wall precursor metabolism." PLoS Genet 10(1);e1004056. PMID: 24391520

Reed03: Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)." Genome Biol 4(9);R54. PMID: 12952533

Silber74: Silber P, Chung H, Gargiulo P, Schulz H (1974). "Purification and properties of a diacetyl reductase from Escherichia coli." J Bacteriol 1974;118(3);919-27. PMID: 4151453

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Van98: Van Dyk TK, Ayers BL, Morgan RW, Larossa RA (1998). "Constricted flux through the branched-chain amino acid biosynthetic enzyme acetolactate synthase triggers elevated expression of genes regulated by rpoS and internal acidification." J Bacteriol 180(4);785-92. PMID: 9473030


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 Sat Nov 22, 2014, biocyc14.