|Gene:||mog||Accession Numbers: EG11511 (EcoCyc), b0009, ECK0009|
Synonyms: yaaG, bisD, chlG, mogA
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 [Liu00].
ChlG: "chlorate resistance"
MogA: "molybdenum cofactor biosynthesis, chlG group [Shanmugam92]
|Map Position: [9,306 -> 9,893] (0.2 centisomes, 1°)||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)
|Biological Process:||GO:0032324 - molybdopterin cofactor biosynthetic process
GO:0006777 - Mo-molybdopterin cofactor biosynthetic process [UniProtGOA11, GOA01]
|Molecular Function:||GO:0000166 - nucleotide binding
GO:0005524 - ATP binding [UniProtGOA11]
GO:0016740 - transferase activity [UniProtGOA11]
GO:0061598 - molybdopterin adenylyltransferase activity [GOA01a]
|Cellular Component:||GO:0005829 - cytosol
GO:0005737 - cytoplasm [Gaudet10]
|MultiFun Terms:||metabolism → biosynthesis of building blocks → cofactors, small molecule carriers → molybdenum|
|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: 188.8.131.52
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
10/20/97 Gene b0009 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11511; confirmed by SwissProt match.
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
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
Liu00: 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
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
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