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Escherichia coli K-12 substr. MG1655 Enzyme: MogA



Gene: mog Accession Numbers: EG11511 (EcoCyc), b0009, ECK0009

Synonyms: yaaG, bisD, chlG, mogA

Regulation Summary Diagram: ?

Summary:
Molybdenum and tungsten cofactors of all enzymes that require one or the other for activity are present in an oxidized state as molybdate or tungstate ions that are chelated by the cis-ditholene moiety of the molybdenum cofactor. The particular cofactor that occurs in Escherichia coli is molybdenum guanine dinucleotide. This and other molydenum cofactors are so extremely unstable that they have not been isolated in pure form and only the outline of their pathway of biosynthesis has been elucidated. In the last step molybdenum is inserted to become chelated by the cis-dithiolene moiety of molybdopterin and a guanyl group is added yielding molybdopterin guanine dinucleotide, the acitve cofactor of E. coli. MogA, along with MoeA, is implicated in the step involving the chelation of molybdenum. [Leimkuhler01]

Crystal structures of MogA have been solved at 1.6 and 1.45 Å resolution, and a putative active site has been identified [Liu00a].

ChlG: "chlorate resistance"

MogA: "molybdenum cofactor biosynthesis, chlG group [Shanmugam92]

Locations: cytosol

Map Position: [9,306 -> 9,893] (0.2 centisomes)
Length: 588 bp / 195 aa

Molecular Weight of Polypeptide: 21.222 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000030 , CGSC:917 , DIP:DIP-35784N , EchoBASE:EB1473 , EcoGene:EG11511 , EcoliWiki:b0009 , Mint:MINT-1238245 , ModBase:P0AF03 , OU-Microarray:b0009 , PortEco:mog , Pride:P0AF03 , Protein Model Portal:P0AF03 , RefSeq:NP_414550 , RegulonDB:EG11511 , SMR:P0AF03 , String:511145.b0009 , Swiss-Model:P0AF03 , UniProt:P0AF03

Relationship Links: InterPro:IN-FAMILY:IPR001453 , InterPro:IN-FAMILY:IPR008284 , InterPro:IN-FAMILY:IPR020817 , PDB:Structure:1DI6 , PDB:Structure:1DI7 , Pfam:IN-FAMILY:PF00994 , Prosite:IN-FAMILY:PS01078 , Smart:IN-FAMILY:SM00852

In Paralogous Gene Group: 3 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0032324 - molybdopterin cofactor biosynthetic process Inferred from experiment [Nichols05]
GO:0006777 - Mo-molybdopterin cofactor biosynthetic process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0061598 - molybdopterin adenylyltransferase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism biosynthesis of building blocks cofactors, small molecule carriers molybdenum

Essentiality data for mog knockouts: ?

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

Enzymatic reaction of: molybdopterin adenylyltransferase (MogA)

EC Number: 2.7.7.75

ATP + molybdopterin + H+ <=> molybdopterin adenine dinucleotide + diphosphate

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.

In Pathways: molybdenum cofactor biosynthesis

Credits:
Imported from MetaCyc 13-Sep-2011 by Caspi R , SRI International


Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 49
[Liu00a, UniProt11a]
Alternate sequence: D → A; UniProt: Loss of activity.
Mutagenesis-Variant 82
[Liu00a, UniProt11a]
Alternate sequence: D → A; UniProt: Loss of activity.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0009 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11511; 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

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.

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

Leimkuhler01: Leimkuhler S, Wuebbens MM, Rajagopalan KV (2001). "Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor." J Biol Chem 276(37);34695-701. PMID: 11463785

Liu00a: Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H (2000). "Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli." J Biol Chem 275(3);1814-22. PMID: 10636880

Nichols05: Nichols JD, Rajagopalan KV (2005). "In vitro molybdenum ligation to molybdopterin using purified components." J Biol Chem 280(9);7817-22. PMID: 15632135

Shanmugam92: Shanmugam KT, Stewart V, Gunsalus RP, Boxer DH, Cole JA, Chippaux M, DeMoss JA, Giordano G, Lin EC, Rajagopalan KV (1992). "Proposed nomenclature for the genes involved in molybdenum metabolism in Escherichia coli and Salmonella typhimurium." Mol Microbiol 6(22);3452-4. PMID: 1484496

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc13.