Escherichia coli K-12 substr. MG1655 Enzyme: molybdopterin adenylyltransferase

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

Synonyms: yaaG, bisD, chlG, mogA

Regulation Summary Diagram: ?

Regulation summary diagram for mog

Subunit composition of molybdopterin adenylyltransferase = [Mog]3
         molybdopterin adenylyltransferase = Mog

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. [Leimkuhler01]

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 [Neumann08]

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 [Stewart82].

ChlG: "chlorate resistance"

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

Reviews: [IobbiNivol13, Rizzi02, Rajagopalan92]

Locations: cytosol

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)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0032324 - molybdopterin cofactor biosynthetic process Inferred from experiment [Liu00a, Nichols05]
GO:0006777 - Mo-molybdopterin cofactor biosynthetic process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Magalon02]
GO:0042802 - identical protein binding Inferred from experiment [Liu00a]
GO:0061598 - molybdopterin adenylyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01, Nichols05]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0005737 - cytoplasm Inferred by computational analysis [Gaudet10]

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]

Created 09-Feb-2015 by Fulcher C , SRI International
Last-Curated ? 09-Feb-2015 by Fulcher C , SRI International

Enzymatic reaction of: molybdopterin adenylyltransferase

EC Number:

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

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

Cofactors or Prosthetic Groups: Mg2+ [Nichols05]

Sequence Features

Protein sequence of molybdopterin adenylyltransferase with features indicated

Feature Class Location Citations Comment
Mutagenesis-Variant 49
[Liu00a, UniProt11a]
UniProt: Loss of activity.
Mutagenesis-Variant 82
[Liu00a, UniProt11a]
UniProt: Loss of activity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

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

Neumann08: 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

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

Rajagopalan92: Rajagopalan KV, Johnson JL (1992). "The pterin molybdenum cofactors." J Biol Chem 267(15);10199-202. PMID: 1587808

Rizzi02: Rizzi M, Schindelin H (2002). "Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis." Curr Opin Struct Biol 12(6);709-20. PMID: 12504674

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

Stewart82: Stewart V, MacGregor CH (1982). "Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci." J Bacteriol 151(2);788-99. PMID: 7047497

Theisen13: Theisen J, Zylstra GJ, Yee N (2013). "Genetic evidence for a molybdopterin-containing tellurate reductase." Appl Environ Microbiol 79(10);3171-5. PMID: 23475618

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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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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 19.0 on Mon Oct 5, 2015, biocyc14.