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MetaCyc Polypeptide: glycolate oxidase, predicted FAD-binding subunit

Gene: glcE Accession Numbers: G7544 (MetaCyc), b4468, ECK2973

Synonyms: yghL, gox, b2978 (obsolete)

Species: Escherichia coli K-12 substr. MG1655

Component of: glycolate oxidase (summary available)

Map Position: [3,123,492 <- 3,124,544]

Molecular Weight of Polypeptide: 38.361 kD (from nucleotide sequence), 40 kD (experimental) [Pellicer96]

Unification Links: ASAP:ABE-0174098, EchoBASE:EB2819, EcoGene:EG12996, EcoliWiki:b4468, ModBase:P52073, PortEco:glcE, Protein Model Portal:P52073, RefSeq:YP_026191, RegulonDB:G7544, SMR:P52073, String:511145.b4468, UniProt:P52073

Relationship Links: InterPro:IN-FAMILY:IPR006094, InterPro:IN-FAMILY:IPR016164, InterPro:IN-FAMILY:IPR016166, InterPro:IN-FAMILY:IPR016169, InterPro:IN-FAMILY:IPR016171, OU-Microarray:RELATED-TO:b2978, Pfam:IN-FAMILY:PF01565, Prosite:IN-FAMILY:PS51387

Gene-Reaction Schematic

Gene-Reaction Schematic

GO Terms:
Biological Process:
Inferred from experimentGO:0046296 - glycolate catabolic process [Pellicer96]
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
Molecular Function:
Inferred from experimentGO:0019154 - glycolate dehydrogenase activity [Pellicer96]
Inferred by computational analysisGO:0003824 - catalytic activity [GOA01a]
Inferred by computational analysisGO:0016491 - oxidoreductase activity [UniProtGOA11a]
Inferred by computational analysisGO:0016614 - oxidoreductase activity, acting on CH-OH group of donors [GOA01a]
Inferred by computational analysisGO:0050660 - flavin adenine dinucleotide binding [GOA01a]

MultiFun Terms: metabolismcentral intermediary metabolismglycolate metabolism

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

Subunit of: glycolate oxidase

Inferred from experiment

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of glycolate oxidase = [GlcD][GlcE][GlcF]
         glycolate oxidase, predicted FAD-linked subunit = GlcD
         glycolate oxidase, predicted FAD-binding subunit = GlcE
         glycolate oxidase, predicted iron-sulfur subunit = GlcF (summary available)

Glycolate oxidase catalyzes the first step in the utilization of glycolate as the sole source of carbon [Lord72]. The enzyme may be membrane-associated; Sallal and Nimer ( [Sallal89]) isolated a cytoplasmic membrane-associated glycolate oxidoreductase activity from E. coli ATCC11775 (serovar O1:K1:H7), and the GlcF subunit itself could only be detected in the membrane fraction [Pellicer96]. The physiological electron acceptor is unknown.

Crude extracts from an E. coli strain expressing glcDEF from a multicopy plasmid contain glycolate oxidase activity. Insertion mutants in either glcD, glcE, or glcF abolish this activity, suggesting that all three gene products are subunits of a glycolate oxidase complex [Pellicer96].

Expression of the glcDEFGB operon is induced by growth on glycolate [Pellicer99].

Created in EcoCyc 30-Nov-2006 by Keseler I, SRI International
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International

Enzymatic reaction of: glycolate oxidase

Inferred from experiment

Synonyms: glycolate oxidoreductase, glycolate:(acceptor) 2-oxidoreductase, glycolate dehydrogenase

EC Number:

glycolate + an oxidized unknown electron acceptor → glyoxylate + an reduced unknown electron acceptor

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Alternative Substrates for glycolate [Lord72]: (R)-lactate [Comment 1, Lord72]

In Pathways: superpathway of glycol metabolism and degradation, glycolate and glyoxylate degradation II, glycolate and glyoxylate degradation I

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

Inhibitors (Unknown Mechanism): Zn2+ [Lord72], copper sulfate [Lord72], p-chloromercuribenzoate [Lord72], Hg2+ [Lord72], potassium cyanide [Lord72]Kinetic Parameters:
Substrate Km (μM) Citations
glycolate 40.0 [Lord72]

pH(opt): 8-8.8 [Lord72]

Sequence Features

Feature Class Location Citations Comment
Conserved-Region 1 -> 173
Inferred by computational analysis[UniProt15]
UniProt: FAD-binding PCMH-type.

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


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

Lord72: Lord JM (1972). "Glycolate oxidoreductase in Escherichia coli." Biochim Biophys Acta 1972;267(2);227-37. PMID: 4557653

Pellicer96: Pellicer MT, Badia J, Aguilar J, Baldoma L (1996). "glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein." J Bacteriol 1996;178(7);2051-9. PMID: 8606183

Pellicer99: Pellicer MT, Fernandez C, Badia J, Aguilar J, Lin EC, Baldom L (1999). "Cross-induction of glc and ace operons of Escherichia coli attributable to pathway intersection. Characterization of the glc promoter." J Biol Chem 274(3);1745-52. PMID: 9880556

Sallal89: Sallal AK, Nimer NA (1989). "The intracellular localization of glycolate oxidoreductase in Escherichia coli." FEBS Lett 1989;258(2);277-80. PMID: 2689218

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

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 Pathway Tools version 19.5 (software by SRI International) on Wed Jan 2, 2002, biocyc12.