Member database | Pfam |
Pfam type | domain |
Short name | MoCoBD_1 |
Clan | DmpA_ArgJ |
Author | Bateman A;0000-0002-6982-4660 Griffiths-Jones SR;0000-0001-6043-807X |
Sequence Ontology | 0000417 |
Description Imported from IPR008274
The aldehyde oxido-reductase (Mop) from the sulphate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas is a homodimer of 907 amino acid residues subunits and is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centres. It is folded into four domains of which the first two bind the iron sulphur centres and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands
[2].
This domain represents the first molybdopterin cofactor (Mo-Co) binding domain.
Aldehyde oxidase (AOX
1.2.3.1) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase (XDH
1.17.1.4) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase (
1.17.3.2) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulfhydryl groups
[1].
References Imported from IPR008274
1.Xanthine dehydrogenase: An old enzyme with new knowledge and prospects. Wang CH, Zhang C, Xing XH. Bioengineered 7, 395-405, (2016). PMID: 27537049
2.Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Romao MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R. Science 270, 1170-6, (1995). View articlePMID: 7502041