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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Polypeptide: anaerobic glycerol-3-phosphate dehydrogenase subunit A

Gene: glpA Accession Numbers: EG10391 (MetaCyc), b2241, ECK2233

Species: Escherichia coli K-12 substr. MG1655

Component of: glycerol-3-phosphate dehydrogenase, anaerobic (extended summary available)

Summary:
GlpA is the large subunit of a three subunit glycerol-3-phosphate dehydrogenase complex. In anaerobic conditions this respiratory enzyme converts glycerol-3-phosphate to dihydroxyacetone phosphate (DHAP) using fumarate as a terminal electron acceptor. The GlpA subunit contains noncovalently bound FAD. [Cole88, Schryvers82, Schryvers81, Kistler71].

Citations: [Iuchi90, Ehrmann87, Miki79a, Freedberg73]

Locations: cytosol, inner membrane

Map Position: [2,350,669 -> 2,352,297]

Molecular Weight of Polypeptide: 58.958 kD (from nucleotide sequence), 62.0 kD (experimental) [Schryvers81 ]

Unification Links: ASAP:ABE-0007422 , CGSC:694 , EchoBASE:EB0386 , EcoGene:EG10391 , EcoliWiki:b2241 , ModBase:P0A9C0 , OU-Microarray:b2241 , PortEco:glpA , PR:PRO_000022792 , Pride:P0A9C0 , Protein Model Portal:P0A9C0 , RefSeq:NP_416744 , RegulonDB:EG10391 , SMR:P0A9C0 , String:511145.b2241 , UniProt:P0A9C0

Relationship Links: InterPro:IN-FAMILY:IPR000447 , InterPro:IN-FAMILY:IPR006076 , InterPro:IN-FAMILY:IPR007419 , InterPro:IN-FAMILY:IPR017752 , Pfam:IN-FAMILY:PF01266 , Pfam:IN-FAMILY:PF04324 , Prints:IN-FAMILY:PR01001 , Prosite:IN-FAMILY:PS00977 , Prosite:IN-FAMILY:PS00978

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Kuritzkes84]
GO:0046168 - glycerol-3-phosphate catabolic process Inferred from experiment [Varga95, Schryvers81]
GO:0006072 - glycerol-3-phosphate metabolic process Inferred by computational analysis [GOA01]
GO:0019563 - glycerol catabolic process Inferred by computational analysis [UniProtGOA12]
GO:0046174 - polyol catabolic process Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0004368 - glycerol-3-phosphate dehydrogenase activity Inferred from experiment Inferred by computational analysis [GOA01, Varga95, Kistler71, Schryvers81]
GO:0005515 - protein binding Inferred from experiment [Schryvers81]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment Inferred by computational analysis [GOA01, Cole88, Schryvers81]
GO:0010181 - FMN binding Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0052591 - sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Schryvers82]
GO:0009331 - glycerol-3-phosphate dehydrogenase complex Inferred from experiment Inferred by computational analysis [GOA01, Varga95]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism central intermediary metabolism misc. glycerol metabolism
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron donors

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


Subunit of: glycerol-3-phosphate dehydrogenase, anaerobic

Synonyms: G3P dehydrogenase, sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of glycerol-3-phosphate dehydrogenase, anaerobic = [GlpA][GlpB][GlpC]
         anaerobic glycerol-3-phosphate dehydrogenase subunit A = GlpA (summary available)
         anaerobic glycerol-3-phosphate dehydrogenase subunit B = GlpB (summary available)
         anaerobic glycerol-3-phosphate dehydrogenase subunit C = GlpC (summary available)

Summary:
glpABC encodes anaerobic glycerol-3-phosphate dehydrogenase which catalyses the oxidation of glycerol-3-phosphate to dihyroxyacetone phosphate. GlpABC is a respiratory enzyme; anaerobic growth of E. coli with glycerol and fumarate induces expression of an anaerobic glycerol-3-phosphate dehydrogenase and fumarate reductase and is associated with proton translocation and the generation of a proton motive force [Miki78, Miki73, Kistler71].

The GlpABC enzyme is loosely associated with the cell membrane. A functional two subunit form, GlpAB, has been isolated and characterised; it is assumed that the third subunit (GlpC) is responsible for membrane anchoring. The GlpAB complex contains contains 1 molecule of FAD and 2 non-haem irons per dimer; the GlpB subunit is thought to bind flavin mononucleotide [Schryvers81, Cole88]. The GlpC subunit contains two iron-sulfur binding sites; it does not contain any transmembrane helices, so the mechanism by which it acts as the membrane anchor for the complex is not clear [Cole88, Varga95]. Overexpressed GlpC associates with the inner membrane. GlpC is a participant in the electron transport path ([Varga95] - note that this paper uses the name GlpB for the protein encoded by the third gene in the glp operon).

glpABC is subject to complex transcriptional regulation. Expression of glpABC (along with other members of the glp regulon) is repressed by GlpR and induced by glycerol-3-phosphate; the glp regulon is subject to catabolite repression during growth in the presence of glucose (reviewed in [Lin76], [Larson92] ). Expression of glpABC is positively regulated by the the Fnr transcription regulator [Kuritzkes84, Iuchi90].

E. coli K-12 contains two glycerol-3-phosphate dehydrogenases encoded by the glpABC and glpD genes. GlpABC is required for anaerobic growth with glycerol or glycerol-3-phosphate and fumarate as the terminal electron acceptor while GlpD is required for aerobic growth with glycerol (or glycerol-3-phosphate). Either enzyme suffices for anaerobic growth on glycerol and nitrate ([Kistler71, Miki75a] and review by [Stewart88]. The ratio of GlpD to GlpABC is high when oxygen or nitrate serves as a terminal electron acceptor and low when fumarate serves this role [Freedberg73].

Citations: [Yang97]

Locations [Comment 1]: cytosol

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Kistler71, Miki78]
GO:0046168 - glycerol-3-phosphate catabolic process Inferred from experiment [Schryvers81]
Molecular Function: GO:0004368 - glycerol-3-phosphate dehydrogenase activity Inferred from experiment [Schryvers81]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment [Schryvers81]
Cellular Component: GO:0009331 - glycerol-3-phosphate dehydrogenase complex Inferred from experiment [Varga95]

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


Enzymatic reaction of: glycerol-3-phosphate dehydrogenase, anaerobic

Synonyms: G3P dehydrogenase, sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase

In Pathways: glycerol-3-phosphate to fumarate electron transfer

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

Cofactors or Prosthetic Groups: FAD [Schryvers81], FMN [Schryvers81]

Inhibitors (Unknown Mechanism): p-chloromercuriphenylsulfonate [Schryvers81] , 5,5'-dithio-bis-2-nitrobenzoate [Schryvers81]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
sn-glycerol 3-phosphate
100.0, 339.0
33.3
[Schryvers81, BRENDA14]

T(opt): 44 °C [BRENDA14, Schryvers78]

pH(opt): 7 [BRENDA14, Schryvers78]


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 10 -> 38
[UniProt10a]
UniProt: FAD; Non-Experimental Qualifier: potential;
Sequence-Conflict 329
[Cole88, UniProt10]
Alternate sequence: L; UniProt: (in Ref. 1; AAA83864);

History:
10/20/97 Gene b2241 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10391; confirmed by SwissProt match.


References

Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Cole88: Cole ST, Eiglmeier K, Ahmed S, Honore N, Elmes L, Anderson WF, Weiner JH (1988). "Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12." J Bacteriol 1988;170(6);2448-56. PMID: 3286606

Ehrmann87: Ehrmann M, Boos W, Ormseth E, Schweizer H, Larson TJ (1987). "Divergent transcription of the sn-glycerol-3-phosphate active transport (glpT) and anaerobic sn-glycerol-3-phosphate dehydrogenase (glpA glpC glpB) genes of Escherichia coli K-12." J Bacteriol 169(2);526-32. PMID: 3027032

Freedberg73: Freedberg WB, Lin EC (1973). "Three kinds of controls affecting the expression of the glp regulon in Escherichia coli." J Bacteriol 115(3);816-23. PMID: 4580569

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

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Iuchi90: Iuchi S, Cole ST, Lin EC (1990). "Multiple regulatory elements for the glpA operon encoding anaerobic glycerol-3-phosphate dehydrogenase and the glpD operon encoding aerobic glycerol-3-phosphate dehydrogenase in Escherichia coli: further characterization of respiratory control." J Bacteriol 172(1);179-84. PMID: 2403539

Kistler71: Kistler WS, Lin EC (1971). "Anaerobic L- -glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role." J Bacteriol 108(3);1224-34. PMID: 4945192

Kuritzkes84: Kuritzkes DR, Zhang XY, Lin EC (1984). "Use of phi(glp-lac) in studies of respiratory regulation of the Escherichia coli anaerobic sn-glycerol-3-phosphate dehydrogenase genes (glpAB)." J Bacteriol 157(2);591-8. PMID: 6363389

Larson92: Larson TJ, Cantwell JS, van Loo-Bhattacharya AT (1992). "Interaction at a distance between multiple operators controls the adjacent, divergently transcribed glpTQ-glpACB operons of Escherichia coli K-12." J Biol Chem 267(9);6114-21. PMID: 1556120

Lin76: Lin EC (1976). "Glycerol dissimilation and its regulation in bacteria." Annu Rev Microbiol 1976;30;535-78. PMID: 825019

Miki73: Miki K, Lin EC (1973). "Enzyme complex which couples glycerol-3-phosphate dehydrogenation to fumarate reduction in Escherichia coli." J Bacteriol 114(2);767-71. PMID: 4574699

Miki75a: Miki K, Lin EC (1975). "Electron transport chain from glycerol 3-phosphate to nitrate in Escherichia coli." J Bacteriol 124(3);1288-94. PMID: 127786

Miki78: Miki K, Wilson TH (1978). "Proton translocation associated with anaerobic transhydrogenation from glycerol 3-phosphate to fumarate in Escherichia coli." Biochem Biophys Res Commun 83(4);1570-5. PMID: 29636

Miki79a: Miki K, Silhavy TJ, Andrews KJ (1979). "Resolution of glpA and glpT loci into separate operons in Escherichia coli K-12 strains." J Bacteriol 138(1);268-9. PMID: 374371

Schryvers78: Schryvers A, Lohmeier E, Weiner JH (1978). "Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli." J Biol Chem 253(3);783-8. PMID: 340460

Schryvers81: Schryvers A, Weiner JH (1981). "The anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli. Purification and characterization." J Biol Chem 1981;256(19);9959-65. PMID: 6792201

Schryvers82: Schryvers A, Weiner JH (1982). "The anaerobic sn-glycerol-3-phosphate dehydrogenase: cloning and expression of the glpA gene of Escherichia coli and identification of the glpA products." Can J Biochem 60(3);224-31. PMID: 6282417

Stewart88: Stewart V (1988). "Nitrate respiration in relation to facultative metabolism in enterobacteria." Microbiol Rev 52(2);190-232. PMID: 3045516

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: 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."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Varga95: Varga ME, Weiner JH (1995). "Physiological role of GlpB of anaerobic glycerol-3-phosphate dehydrogenase of Escherichia coli." Biochem Cell Biol 73(3-4);147-53. PMID: 7576488

Yang97: Yang B, Gerhardt SG, Larson TJ (1997). "Action at a distance for glp repressor control of glpTQ transcription in Escherichia coli K-12." Mol Microbiol 24(3);511-21. PMID: 9179845


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 Mon Dec 22, 2014, BIOCYC14B.