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MetaCyc Polypeptide: glycolate oxidase, predicted FAD-linked subunit

Gene: glcD Accession Numbers: G7545 (MetaCyc), b2979, ECK2974

Synonyms: yghM, gox

Species: Escherichia coli K-12 substr. MG1655

Component of: glycolate oxidase (summary available)

Locations: cytosol

Map Position: [3,124,544 <- 3,126,043]

Molecular Weight of Polypeptide: 53.812 kD (from nucleotide sequence), 56 kD (experimental) [Pellicer96 ]

Unification Links: ASAP:ABE-0009773 , EchoBASE:EB2820 , EcoGene:EG12997 , EcoliWiki:b2979 , ModBase:P0AEP9 , OU-Microarray:b2979 , PortEco:glcD , Protein Model Portal:P0AEP9 , RefSeq:NP_417453 , RegulonDB:G7545 , SMR:P0AEP9 , String:511145.b2979 , UniProt:P0AEP9

Relationship Links: InterPro:IN-FAMILY:IPR004113 , InterPro:IN-FAMILY:IPR004490 , InterPro:IN-FAMILY:IPR006094 , InterPro:IN-FAMILY:IPR016164 , InterPro:IN-FAMILY:IPR016166 , InterPro:IN-FAMILY:IPR016167 , InterPro:IN-FAMILY:IPR016169 , InterPro:IN-FAMILY:IPR016171 , Pfam:IN-FAMILY:PF01565 , Pfam:IN-FAMILY:PF02913 , Prosite:IN-FAMILY:PS51387

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0046296 - glycolate catabolic process Inferred from experiment [Pellicer96]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0019154 - glycolate dehydrogenase activity Inferred from experiment [Pellicer96]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0008762 - UDP-N-acetylmuramate dehydrogenase activity Inferred by computational analysis [GOA01]
GO:0008891 - glycolate oxidase activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016614 - oxidoreductase activity, acting on CH-OH group of donors Inferred by computational analysis [GOA01]
GO:0050660 - flavin adenine dinucleotide binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0009339 - glycolate oxidase complex Inferred by computational analysis [GOA01]

MultiFun Terms: metabolism central intermediary metabolism glycolate metabolism

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

Subunit of: glycolate oxidase

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 16-Sep-2014 by Paley S , SRI International

Enzymatic reaction of: glycolate oxidase

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

EC Number:

glycolate + an oxidized electron acceptor <=> glyoxylate + a reduced electron acceptor

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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 16-Sep-2014 by Paley S , SRI International

Inhibitors (Unknown Mechanism): Zn2+ [Lord72] , copper sulfate [Lord72] , p-chloromercuribenzoate [Lord72] , Hg2+ [Lord72] , potassium cyanide [Lord72]

Kinetic Parameters:

Km (μM)

pH(opt): 8-8.8 [Lord72]

Sequence Features

Feature Class Location Citations Comment
Conserved-Region 52 -> 230
UniProt: FAD-binding PCMH-type;

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

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

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

UniProtGOA11: 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 Mar 5, 2015, BIOCYC11A.