InterPro : IPR009036

Name  Molybdenum cofactor biosynthesis, MoeB Short Name  Molybdenum_cofac_synth_MoeB
Type  Domain Description  The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes function as oxidoreductases in carbon, nitrogen, and sulphur metabolism [, ]. In Escherichia coli, biosynthesis of MoCF is a three stage process. It begins with the MoaA and MoaC conversion of GTP to the meta-stable pterin intermediate precursor Z. The second stage involves MPT synthase (MoaD and MoaE), which converts precursor Z to MPT; MoeB is involved in the recycling of MPT synthase. The final step in MoCF synthesis is the attachment of mononuclear Mo to MPT, a process that requires MoeA and which is enhanced by MogA in an Mg2 ATP-dependent manner []. MoCF is the active co-factor in eukaryotic and some prokaryotic molybdo-enzymes, but the majority of bacterial enzymes requiring MoCF, need a modification of MTP for it to be active; MobA is involved in the attachment of a nucleotide monophosphate to MPT resulting in the MGD co-factor, the active co-factor for most prokaryotic molybdo-enzymes. Bacterial two-hybrid studies have revealed the close interactions between MoeA, MogA, and MobA in the synthesis of MoCF []. Moreover the close functional association of MoeA and MogA in the synthesis of MoCF is supported by fact that the known eukaryotic homologues to MoeA and MogA exist as fusion proteins: CNX1 () of Arabidopsis thaliana(Mouse-ear cress), mammalian Gephryin (e.g. ) and Drosophila melanogaster(Fruit fly) Cinnamon () [].The Escherichia coliprotein is involved in molybdenum cofactor (MoCF) biosynthesis, an evolutionarily conserved pathway. MoeB activates the C terminus of MoaD to form an acyl-adenylate, which is subsequently converted to a thiocarboxylate that acts as the sulphur donor during Moco biosynthesis. The structure of MoeB consists of a three-layer sandwich of alpha/beta/alpha []. The sandwich is composed of eight beta-strands, which form a continuous mixed beta sheet in the order 32145678 surrounded by eight helices. Beta strands 6 and 8 are antiparallel to the rest. The N-terminal half of the sheet contains the ATP nucleotide-binding site, which is similar to that of the NAD-binding Rossmann fold. A loop between beta-1 and alpha-3 contains a glycine-rich motif similar to the P loop found in enzymes that hydrolyse ATP. The C-terminal half of the sheet contains a fold that is similar to that found in a family of sugar-binding proteins.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

6 Contains

Id Name Short Name Type
IPR000594 UBA/THIF-type NAD/FAD binding fold ThiF_NAD_FAD-bd Domain
IPR014929 E2 binding E2_binding Domain
IPR019572 Ubiquitin-activating enzyme Ubiquitin-activating_enzyme Domain
IPR018074 Ubiquitin-activating enzyme, E1, active site UBQ-activ_enz_E1_AS Active_site
IPR000127 Ubiquitin-activating enzyme repeat UBact_repeat Repeat
IPR007901 MoeZ/MoeB MoeZ_MoeB Domain

7 Found In

Id Name Short Name Type
IPR006285 Ubiquitin-like modifier-activating enzyme Atg7 Atg7 Family
IPR000011 Ubiquitin/SUMO-activating enzyme E1 UBQ/SUMO-activ_enz_E1-like Family
IPR018075 Ubiquitin-activating enzyme, E1 UBQ-activ_enz_E1 Family
IPR012731 Thiazole biosynthesis adenylyltransferase ThiF Adenyl_ThiF Family
IPR012729 Thiamine biosynthesis protein ThiF ThiF_fam2 Family
IPR012730 Molybdopterin synthase sulfurylase MoeB Mopterin_Synthase_Sase_MoeB Family
IPR022368 Putative thiazole-containing bacteriocin maturation protein Thiazole_bacteriocin_mat_put Family

1 Parent Features

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain

6 Publications

First Author Title Year Journal Volume Pages
Magalon A In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli. 2002 J Biol Chem 277 48199-204
Stallmeyer B Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three Escherichia coli proteins. 1995 Plant J 8 751-62
Hille R Molybdenum and tungsten in biology. 2002 Trends Biochem Sci 27 360-7
Nichols JD Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. 2007 Biochemistry 46 78-86
Mendel RR Cell biology of molybdenum. 2006 Biochim Biophys Acta 1763 621-35
Lake MW Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. 2001 Nature 414 325-9



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)