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

Fe-ADH
PFAM accession number:PF00465
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:

  • Zinc-containing 'long-chain' alcohol dehydrogenases.
  • Insect-type, or 'short-chain' alcohol dehydrogenases.
  • Iron-containing alcohol dehydrogenases.

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:

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 Fe-ADH