|Gene:||mog||Accession Numbers: EG11511 (EcoCyc), b0009, ECK0009|
Synonyms: yaaG, bisD, chlG, mogA
Molybdenum and tungsten cofactors of all enzymes (except nitrogenase) 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-dithiolene moiety of a molybdenum cofactor. The cofactor that predominates in E. coli is molybdopterin guanine dinucleotide. Although much progress has been made in elucidating the biosynthetic pathways for molybdenum cofactors (see the [IobbiNivol13] review), some details remain to be determined. 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 active cofactor of E. coli. MogA, along with MoeA, is implicated in the step involving the chelation of molybdenum. [Leimkuhler01a]
Crystal structures of MogA have been solved at 1.6 Å and 1.45 Å resolution, and a putative active site has been identified. In two crystal forms studied the MogA monomers formed a trimeric arrangement. Analytical ultracentrifugation data showed a native molecular mass of 59,675 Da, consistent with a trimeric structure in solution [Liu00a].
Studies using a bacterial two-hybrid system showed that MogA directly interacts with MoeA and MobB in vivo [Magalon02]. In the presence of the enzyme-specific chaperone NarJ and the mature molybdenum cofactor, MobA, MobB, MoeA and MogA interact with apo-NarG [Vergnes04].
In E. coli K-12, mog (mogA), moaA, moaB, moaE, modB, or modC deletion mutants lose the ability to reduce tellurite (tellurate), which can be restored by complementation. Although the E. coli tellurate reductase gene and its product remain uncharacterized, these data suggest that it involves a molybdoenzyme [Theisen13].
Data suggest that in the presence of physiological concentrations of molybdate, both MogA and MoeA are required to form the molybdopterin adenine dinucleotide intermediate in E. coli, whereas under high molybdate concentrations MogA is not required. Some heavy metals at high concentrations can be nonspecifically inserted into the MoO2-cofactor independent of both MogA and MoeA, resulting in inhibition of molybdoenzyme activity [Neumann08a]
Functional homologs of E. coli MogA with molybdopterin adenylyltransferase activity include the archaeal MoaB and the eukaryotic Cnx1G domain. An E. coli mogA mutant could be complemented by moaB from the archaeon Pyrococcus furiosus [Bevers08].
Early mutant studies of nitrate reductase activity in E. coli K-12 identified the involvement of chlG (mog) in molybdenum cofactor synthesis or insertion [Stewart82a].
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)
Molecular Weight of Multimer: 59.675 kD (experimental) [Liu00a]
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 [UniProtGOA11a, GOA01a]
|Molecular Function:||GO:0005515 - protein binding
GO:0042802 - identical protein binding [Liu00a]
GO:0061598 - molybdopterin adenylyltransferase activity [GOA01, Nichols05]
GO:0000166 - nucleotide binding [UniProtGOA11a]
GO:0005524 - ATP binding [UniProtGOA11a]
GO:0016740 - transferase activity [UniProtGOA11a]
|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
EC Number: 18.104.22.168
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
Bevers08: Bevers LE, Hagedoorn PL, Santamaria-Araujo JA, Magalon A, Hagen WR, Schwarz G (2008). "Function of MoaB proteins in the biosynthesis of the molybdenum and tungsten cofactors." Biochemistry 47(3);949-56. PMID: 18154309
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
IobbiNivol13: Iobbi-Nivol C, Leimkuhler S (2013). "Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli." Biochim Biophys Acta 1827(8-9);1086-101. PMID: 23201473
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
Leimkuhler01a: 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
Magalon02: Magalon A, Frixon C, Pommier J, Giordano G, Blasco F (2002). "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli." J Biol Chem 277(50);48199-204. PMID: 12372836
Neumann08a: Neumann M, Leimkuhler S (2008). "Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli." FEBS J 275(22);5678-89. PMID: 18959753
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
Vergnes04: Vergnes A, Gouffi-Belhabich K, Blasco F, Giordano G, Magalon A (2004). "Involvement of the molybdenum cofactor biosynthetic machinery in the maturation of the Escherichia coli nitrate reductase A." J Biol Chem 279(40);41398-403. PMID: 15247236
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