The domain within your query sequence starts at position 91 and ends at position 165; the E-value for the Fer2_2 domain shown below is 1e-29.
TVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGN LCRCTGYRPIVESAK
Fer2_2 |
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| PFAM accession number: | PF01799 |
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| Interpro abstract (IPR002888): | The [2Fe-2S] binding domain is found in a range of enzymes including dehydrogenases, oxidases and oxidoreductases. 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 [ (PUBMED:7502041) ]. |
| GO process: | oxidation-reduction process (GO:0055114) |
| GO function: | metal ion binding (GO:0046872), oxidoreductase activity (GO:0016491) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Fer2_2