Sequence of ADHA_GLUOX
EC Number:1.1.5.5
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ethanol + ubiquinone = acetaldehyde + ubiquinol
Other sequences found for EC No. 1.1.5.5
General information:
Sequence
0 MTSGLLTPIK VTKKRLLSCA AALAFSAAVP VAFAQEDTGT AITSSDNGGH PGDWLSYGRS
60 YSEQRYSPLD QINTENVGKL KLAWHYDLDT NRGQEGTPLI VNGVMYATTN WSKMKALDAA
120 TGKLLWSYDP KVPGNIADRG CCDTVSRGAA YWNGKVYFGT FDGRLIALDA KTGKLVWSVY
180 TIPKEAQLGH QRSYTVDGAP RIAKGKVLIG NGGAEFGARG FVSAFDAETG KLDWRFFTVP
240 NPENKPDGAA SDDILMSKAY PTWGKNGAWK QQGGGGTVWD SLVYDPVTDL VYLGVGNGSP
300 WNYKFRSEGK GDNLFLGSIV AINPDTGKYV WHFQETPMDE WDYTSVQQIM TLDMPVNGEM
360 RHVIVHAPKN GFFYIIDAKT GKFITGKPYT YENWANGLDP VTGRPNYVPD ALWTLTGKPW
420 LGIPGELGGH NFAAMAYSPK TKLVYIPAQQ IPLLYDGQKG GFKAYHDAWN LGLDMNKIGL
480 FDDNDPEHVA AKKDFLKVLK GWTVAWDPEK MAPAFTINHK GPWNGGLLAT AGNVIFQGLA
540 NGEFHAYDAT NGNDLYSFPA QSAIIAPPVT YTANGKQYVA VEVGWGGIYP FLYGGVARTS
600 GWTVNHSRVI AFSLDGKDSL PPKNELGFTP VKPVPTYDEA RQKDGYFMYQ TFCSACHGDN
660 AISGGVLPDL RWSGAPRGRE SFYKLVGRGA LTAYGMDRFD TSMTPEQIED IRNFIVKRAN
720 ESYDDEVKAR ENSTGVPNDQ FLNVPQSTAD VPTADHP
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
261950
Kondo K.,Horinouchi S.
Characterization of the genes encoding the three-component membrane-bound alcohol dehydrogenase from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus.
Appl. Environ. Microbiol.
63
1131-1138
1997
261951
Prust C.,Hoffmeister M.,Liesegang H.,Wiezer A.,Fricke W.F.,Ehrenreich A.,Gottschalk G.,Deppenmeier U.
Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans.
Nat. Biotechnol.
23
195-200
2005
261952
Matsushita K.,Nagatani Y.,Shinagawa E.,Adachi O.,Ameyama M.
Reconstitution of the ethanol oxidase respiratory chain in membranes of quinoprotein alcohol dehydrogenase-deficient Gluconobacter suboxydans subsp. alpha strains.
J. Bacteriol.
173
3440-3445
1991
261953
Matsushita K.,Yakushi T.,Takaki Y.,Toyama H.,Adachi O.
Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans.
J. Bacteriol.
177
6552-6559
1995
261954
Matsushita K.,Yakushi T.,Toyama H.,Shinagawa E.,Adachi O.
Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans.
J. Biol. Chem.
271
4850-4857
1996
261955
Matsushita K.,Yakushi T.,Toyama H.,Adachi O.,Miyoshi H.,Tagami E.,Sakamoto K.
The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has ubiquinol oxidation activity at a site different from the ubiquinone reduction site.
Biochim. Biophys. Acta
1409
154-164
1999
261956
Matsushita K.,Kobayashi Y.,Mizuguchi M.,Toyama H.,Adachi O.,Sakamoto K.,Miyoshi H.
A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans.
Biosci. Biotechnol. Biochem.
72
2723-2731
2008
