The domain within your query sequence starts at position 50 and ends at position 454; the E-value for the Fe-ADH domain shown below is 2.1e-105.
SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVR VEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYVNAPIGKG KPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHM PCQVVANSGFDVLCHALESYTAIPYSMRSPCPSNPIQRPAYQGSNPISDIWAVHALQIVA KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVD HPLVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFL FDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDL
Fe-ADH |
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PFAM accession number: | PF00465 |
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Interpro abstract (IPR001670): | Alcohol dehydrogenase ( EC 1.1.1.1 ) (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD. Currently three, structurally and catalytically, different types of alcohol dehydrogenases are known:
Iron-containing ADH's have been found in yeast (gene ADH4) [ (PUBMED:3584063) ], as well as in Zymomonas mobilis (gene adhB) [ (PUBMED:2823079) ]. These two iron-containing ADH's are closely related to the following enzymes:
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GO process: | oxidation-reduction process (GO:0055114) |
GO function: | oxidoreductase activity (GO:0016491), metal ion binding (GO:0046872) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Fe-ADH