InterPro : IPR012182

Name  Bifunctional molybdenum cofactor biosynthesis MobB/MoeA Short Name  MobB_MoeA
Type  Family 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 knowneukaryotic 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 () [].This group represents a predicted bifunctional molybdenum cofactor biosynthesis protein MobB/MoeA.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

5 Contains

Id Name Short Name Type
IPR001453 Molybdopterin binding domain Mopterin-bd_dom Domain
IPR005111 MoeA, C-terminal, domain IV MoeA_C_domain_IV Domain
IPR005110 MoeA, N-terminal and linker domain MoeA_linker/N Domain
IPR020817 Molybdenum cofactor synthesis Mo_cofactor_synthesis Domain
IPR004435 Molybdopterin-guanine dinucleotide biosynthesis protein B (MobB) domain MobB_dom Domain

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0 Parent Features

5 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



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)