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Alcohol dehydrogenase class-P (AtADH) (EC 1.1.1.1)

 ADH1_ARATH              Reviewed;         379 AA.
P06525; O04080; O04713; O04717; O04868; O23821; Q8LA61; Q94AY6;
Q9CAZ2; Q9CAZ3; Q9SX08;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
22-NOV-2017, entry version 161.
RecName: Full=Alcohol dehydrogenase class-P {ECO:0000305};
Short=AtADH {ECO:0000303|PubMed:25447145};
EC=1.1.1.1 {ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754};
Name=ADH1 {ECO:0000303|PubMed:3377754};
Synonyms=ADH {ECO:0000303|PubMed:2937058};
OrderedLocusNames=At1g77120 {ECO:0000312|Araport:AT1G77120};
ORFNames=F22K20.19 {ECO:0000312|EMBL:AAC00625.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY
2,4-DICHLOROPHENOXYACETIC ACID.
PubMed=2937058; DOI=10.1073/pnas.83.5.1408;
Chang C., Meyerowitz E.M.;
"Molecular cloning and DNA sequence of the Arabidopsis thaliana
alcohol dehydrogenase gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:1408-1412(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=7851777;
Hanfstingl U., Berry A., Kellogg E.A., Costa J.T. III, Ruediger W.,
Ausubel F.M.;
"Haplotypic divergence coupled with lack of diversity at the
Arabidopsis thaliana alcohol dehydrogenase locus: roles for both
balancing and directional selection?";
Genetics 138:811-828(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Al-0, cv. Bl-1, cv. Bla-10, cv. Bs-0, cv. Chi-0, cv. Ci-0,
cv. Es-0, cv. Gr-1, cv. Ita-0, and cv. Yo-0;
PubMed=8844162;
Innan H., Tajima F., Terauchi R., Miyashita N.T.;
"Intragenic recombination in the Adh locus of the wild plant
Arabidopsis thaliana.";
Genetics 143:1761-1770(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Aa-0, cv. Hiroshima, cv. Mt-0, cv. Pog-0, and cv. Shokei;
PubMed=8587508; DOI=10.1093/oxfordjournals.molbev.a025603;
Miyashita N.T., Innan H., Terauchi R.;
"Intra- and interspecific variation of the alcohol dehydrogenase locus
region in wild plants Arabis gemmifera and Arabidopsis thaliana.";
Mol. Biol. Evol. 13:433-436(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11018155; DOI=10.1093/oxfordjournals.molbev.a026248;
Koch M.A., Haubold B., Mitchell-Olds T.;
"Comparative evolutionary analysis of chalcone synthase and alcohol
dehydrogenase loci in Arabidopsis, Arabis, and related genera
(Brassicaceae).";
Mol. Biol. Evol. 17:1483-1498(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Cvi-0, and cv. Kas-1;
PubMed=11158375; DOI=10.1093/oxfordjournals.molbev.a003790;
Miyashita N.T.;
"DNA variation in the 5' upstream region of the Adh locus of the wild
plants Arabidopsis thaliana and Arabis gemmifera.";
Mol. Biol. Evol. 18:164-171(2001).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. C24;
Santos D.;
"Post-transcriptional silencing of the Arabidopsis adh1 gene triggered
by a fully homologous transgene.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[9]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-101 AND
LYS-106.
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-331.
STRAIN=cv. Columbia;
PubMed=10382288; DOI=10.1139/gen-42-3-387;
Brunel D., Froger N., Pelletier G.;
"Development of amplified consensus genetic markers (ACGM) in Brassica
napus from Arabidopsis thaliana sequences of known biological
function.";
Genome 42:387-402(1999).
[13]
DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-105, AND CATALYTIC ACTIVITY.
STRAIN=cv. Be-0, and cv. Ts-1;
PubMed=3377754; DOI=10.1007/BF00555492;
Jacobs M., Dolferus R., Van den Bossche D.;
"Isolation and biochemical analysis of ethyl methanesulfonate-induced
alcohol dehydrogenase null mutants of arabidopsis thaliana (L.)
Heynh.";
Biochem. Genet. 26:105-122(1988).
[14]
MUTAGENESIS OF CYS-105.
STRAIN=cv. Be-0;
PubMed=2277648; DOI=10.1007/BF00271565;
Dolferus R., van den Bossche D., Jacobs M.;
"Sequence analysis of two null-mutant alleles of the single
Arabidopsis Adh locus.";
Mol. Gen. Genet. 224:297-302(1990).
[15]
INDUCTION BY COLD.
STRAIN=cv. Landsberg erecta;
PubMed=12231733; DOI=10.1104/pp.101.3.833;
Jarillo J.A., Leyva A., Salinas J., Martinez-Zapater J.M.;
"Low temperature induces the accumulation of alcohol dehydrogenase
mRNA in Arabidopsis thaliana, a chilling-tolerant plant.";
Plant Physiol. 101:833-837(1993).
[16]
INDUCTION BY HYPOXIA; ABSCISIC ACID; DEHYDRATION AND COLD.
STRAIN=cv. C24;
PubMed=8787023; DOI=10.1104/pp.111.2.381;
de Bruxelles G.L., Peacock W.J., Dennis E.S., Dolferus R.;
"Abscisic acid induces the alcohol dehydrogenase gene in
Arabidopsis.";
Plant Physiol. 111:381-391(1996).
[17]
ENZYME REGULATION, AND INDUCTION BY HYPOXIA.
PubMed=9522467; DOI=10.1093/oxfordjournals.pcp.a029129;
Porterfield D.M., Crispi M.L., Musgrave M.E.;
"Changes in soluble sugar, starch, and alcohol dehydrogenase in
Arabidopsis thaliana exposed to N2 diluted atmospheres.";
Plant Cell Physiol. 38:1354-1358(1997).
[18]
INDUCTION BY MYB2; ABSCISIC ACID; DEHYDRATION; COLD AND HYPOXIA, AND
TISSUE SPECIFICITY.
PubMed=9611167;
Hoeren F.U., Dolferus R., Wu Y., Peacock W.J., Dennis E.S.;
"Evidence for a role for AtMYB2 in the induction of the Arabidopsis
alcohol dehydrogenase gene (ADH1) by low oxygen.";
Genetics 149:479-490(1998).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. C24;
PubMed=9880346; DOI=10.1104/pp.119.1.57;
Ellis M.H., Dennis E.S., Peacock W.J.;
"Arabidopsis roots and shoots have different mechanisms for hypoxic
stress tolerance.";
Plant Physiol. 119:57-64(1999).
[20]
INDUCTION BY SPACEFLIGHT AND HYPOXIA.
STRAIN=cv. Wassilewskija;
PubMed=11402191; DOI=10.1104/pp.126.2.613;
Paul A.-L., Daugherty C.J., Bihn E.A., Chapman D.K., Norwood K.L.L.,
Ferl R.J.;
"Transgene expression patterns indicate that spaceflight affects
stress signal perception and transduction in arabidopsis.";
Plant Physiol. 126:613-621(2001).
[21]
INDUCTION BY HYPOXIA.
PubMed=11402202; DOI=10.1104/pp.126.2.742;
Peng H.P., Chan C.S., Shih M.C., Yang S.F.;
"Signaling events in the hypoxic induction of alcohol dehydrogenase
gene in Arabidopsis.";
Plant Physiol. 126:742-749(2001).
[22]
INDUCTION BY HYPOXIA, HIGH SALT, COLD, AND ABCISSIC ACID.
PubMed=11987307;
Manak M.S., Paul A.L., Sehnke P.C., Ferl R.J.;
"Remote sensing of gene expression in Planta: transgenic plants as
monitors of exogenous stress perception in extraterrestrial
environments.";
Life Support Biosph. Sci. 8:83-91(2002).
[23]
INDUCTION BY OXYGEN DEPRIVATION AND CAFFEINE, AND DISRUPTION
PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=12509334; DOI=10.1093/aob/mcf119;
Baxter-Burrell A., Chang R., Springer P., Bailey-Serres J.;
"Gene and enhancer trap transposable elements reveal oxygen
deprivation-regulated genes and their complex patterns of expression
in Arabidopsis.";
Ann. Bot. 91:129-141(2003).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. C24;
PubMed=12857811; DOI=10.1104/pp.103.022244;
Ismond K.P., Dolferus R., de Pauw M., Dennis E.S., Good A.G.;
"Enhanced low oxygen survival in Arabidopsis through increased
metabolic flux in the fermentative pathway.";
Plant Physiol. 132:1292-1302(2003).
[25]
GLUTATHIONYLATION.
STRAIN=cv. Columbia;
PubMed=16055689; DOI=10.1104/pp.104.058917;
Dixon D.P., Skipsey M., Grundy N.M., Edwards R.;
"Stress-induced protein S-glutathionylation in Arabidopsis.";
Plant Physiol. 138:2233-2244(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[27]
INDUCTION BY ABSCISIC ACID; ESTRADIOL; NACL; H2O2 AND SUCROSE.
PubMed=18441225; DOI=10.1104/pp.108.116897;
Papdi C., Abraham E., Joseph M.P., Popescu C., Koncz C., Szabados L.;
"Functional identification of Arabidopsis stress regulatory genes
using the controlled cDNA overexpression system.";
Plant Physiol. 147:528-542(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[29]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20508152; DOI=10.1073/pnas.0914991107;
Zhang F., Maeder M.L., Unger-Wallace E., Hoshaw J.P., Reyon D.,
Christian M., Li X., Pierick C.J., Dobbs D., Peterson T., Joung J.K.,
Voytas D.F.;
"High frequency targeted mutagenesis in Arabidopsis thaliana using
zinc finger nucleases.";
Proc. Natl. Acad. Sci. U.S.A. 107:12028-12033(2010).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[31]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMER, AND CATALYTIC
ACTIVITY.
PubMed=23707506; DOI=10.1016/j.pep.2013.05.004;
Cheng F., Hu T., An Y., Huang J., Xu Y.;
"Purification and enzymatic characterization of alcohol dehydrogenase
from Arabidopsis thaliana.";
Protein Expr. Purif. 90:74-77(2013).
[32]
INDUCTION BY HYDROGEN PEROXIDE.
STRAIN=cv. Columbia;
PubMed=24395201; DOI=10.1007/s00425-013-2020-z;
Yang C.-Y.;
"Hydrogen peroxide controls transcriptional responses of ERF73/HRE1
and ADH1 via modulation of ethylene signaling during hypoxic stress.";
Planta 239:877-885(2014).
[33]
INDUCTION BY WATER SUBMERGENCE.
PubMed=26566261; DOI=10.1080/15548627.2015.1112483;
Chen L., Liao B., Qi H., Xie L.J., Huang L., Tan W.J., Zhai N.,
Yuan L.B., Zhou Y., Yu L.J., Chen Q.F., Shu W., Xiao S.;
"Autophagy contributes to regulation of the hypoxia response during
submergence in Arabidopsis thaliana.";
Autophagy 11:2233-2246(2015).
[34]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 6-379 IN COMPLEX WITH NAD;
SUBSTRATE AND ZINC, COFACTOR, AND HOMODIMER.
PubMed=25447145; DOI=10.1016/j.biochi.2014.10.023;
Chen F., Wang P., An Y., Huang J., Xu Y.;
"Structural insight into the conformational change of alcohol
dehydrogenase from Arabidopsis thaliana L. during coenzyme binding.";
Biochimie 108:33-39(2015).
-!- FUNCTION: Alcohol dehydrogenase mostly active on ethanol (EtOH),
but exhibits broad substrates selectivity for primary and
secondary alcohols (e.g. butanol, propyl alcohol, pentanol,
isopentanol, ethylene glycol, isopropanol, methanol and tertiary
butyl alcohol) (PubMed:23707506). Converts allyl alcohol to highly
toxic acryl-aldehyde (PubMed:20508152). Required for survival and
acclimation in hypoxic conditions, especially in roots
(PubMed:12857811, PubMed:9880346). {ECO:0000269|PubMed:12857811,
ECO:0000269|PubMed:20508152, ECO:0000269|PubMed:23707506,
ECO:0000269|PubMed:9880346}.
-!- CATALYTIC ACTIVITY: A primary alcohol + NAD(+) = an aldehyde +
NADH. {ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754}.
-!- CATALYTIC ACTIVITY: A secondary alcohol + NAD(+) = a ketone +
NADH. {ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:25447145};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:25447145};
-!- ENZYME REGULATION: Alcohol dehydrogenase activity show inverse
correlation with the decreasing availability of oxygen.
{ECO:0000269|PubMed:9522467}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.65 mM for NAD(+) (at pH 10.5 and 25 degrees Celsius)
{ECO:0000269|PubMed:23707506};
KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius)
{ECO:0000269|PubMed:23707506};
Vmax=7.9 umol/min/mg enzyme with NAD(+) as substrate (at pH 10.5
and 25 degrees Celsius) {ECO:0000269|PubMed:23707506};
Vmax=70.1 umol/min/mg enzyme with ethanol as substrate (at pH
10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506};
Note=kcat is 328 min(-1) with NAD(+) as substrate (at pH 10.5
and 25 degrees Celsius). {ECO:0000269|PubMed:23707506};
pH dependence:
Optimum pH is 10.5 (at 25 degrees Celsius).
{ECO:0000269|PubMed:23707506};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23707506,
ECO:0000269|PubMed:25447145}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7851777}.
-!- TISSUE SPECIFICITY: Root specific (PubMed:9611167). Also detected
in etiolated seedlings and leaves in cold conditons
(PubMed:12231733). {ECO:0000269|PubMed:12231733,
ECO:0000269|PubMed:9611167}.
-!- INDUCTION: Transactivated by MYB2 in response to various stresses
(PubMed:9611167). By 2,4-dichlorophenoxyacetic acid (synthetic
auxin) in Arabidopsis as well as in maize (PubMed:2937058).
Induced mostly in roots and shoot apex by hypoxia during water
submergence or oxygen deprivation, in a MYB2-dependent manner, and
partly via an ethylene-mediated pathway (PubMed:9522467,
PubMed:9611167, PubMed:11402202, PubMed:12509334, PubMed:26566261,
PubMed:11987307, PubMed:8787023). Accumulates in response to
hydrogen peroxide H(2)O(2) during the early stages of hypoxia
signaling (PubMed:24395201, PubMed:18441225). Decreased levels
upon combined hypoxia and diphenylene iodonium chloride (DPI, an
NADPH oxidase inhibitor) treatments (PubMed:24395201). Induced by
abscisic acid (ABA), dehydration, estradiol, salt (NaCl), cold and
sucrose treatments (PubMed:12231733, PubMed:18441225,
PubMed:11987307, PubMed:9611167, PubMed:8787023). The induction by
dehydration is ABA-dependent (PubMed:8787023). Observed in
etiolated seedlings and leaves upon exposure to low temperature,
probably via anaerobic metabolism and increase of ABA levels
(PubMed:12231733). Strongly induced by caffeine (PubMed:12509334).
May accumulate in roots during spaceflight, probably due to local
hypoxia conditions (PubMed:11402191).
{ECO:0000269|PubMed:11402191, ECO:0000269|PubMed:11402202,
ECO:0000269|PubMed:11987307, ECO:0000269|PubMed:12231733,
ECO:0000269|PubMed:12509334, ECO:0000269|PubMed:18441225,
ECO:0000269|PubMed:24395201, ECO:0000269|PubMed:26566261,
ECO:0000269|PubMed:8787023, ECO:0000269|PubMed:9522467,
ECO:0000269|PubMed:9611167, ECO:0000303|PubMed:2937058}.
-!- PTM: Glutathionylated. {ECO:0000269|PubMed:16055689}.
-!- DISRUPTION PHENOTYPE: Loss of alcohol dehydrogenase activity
(PubMed:3377754, PubMed:12509334). Increased resistance to allyl
alcohol (PubMed:20508152). Decreased survival, associated with
impaired lateral roots development, upon oxygen deprivation
leading to hypoxic conditions (PubMed:12509334, PubMed:12857811).
Impaired root acclimation to hypoxic stress (PubMed:9880346).
{ECO:0000269|PubMed:12509334, ECO:0000269|PubMed:12857811,
ECO:0000269|PubMed:20508152, ECO:0000269|PubMed:3377754,
ECO:0000269|PubMed:9880346}.
-!- MISCELLANEOUS: Unlike most plants, Arabidopsis contains only one
gene for ADH. {ECO:0000303|PubMed:3377754}.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. Class-P subfamily. {ECO:0000305}.
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EMBL; M12196; AAA32728.1; -; Genomic_DNA.
EMBL; X77943; CAA54911.1; -; Genomic_DNA.
EMBL; D84240; BAA19615.1; -; Genomic_DNA.
EMBL; D84241; BAA19616.1; -; Genomic_DNA.
EMBL; D84242; BAA19617.1; -; Genomic_DNA.
EMBL; D84243; BAA19618.1; -; Genomic_DNA.
EMBL; D84244; BAA19619.1; -; Genomic_DNA.
EMBL; D84245; BAA19620.1; -; Genomic_DNA.
EMBL; D84246; BAA19621.1; -; Genomic_DNA.
EMBL; D84247; BAA19622.1; -; Genomic_DNA.
EMBL; D84248; BAA19623.1; -; Genomic_DNA.
EMBL; D84249; BAA19624.1; -; Genomic_DNA.
EMBL; D63460; BAA22983.1; -; Genomic_DNA.
EMBL; D63461; BAA22979.1; -; Genomic_DNA.
EMBL; D63462; BAA22980.1; -; Genomic_DNA.
EMBL; D63463; BAA22981.1; -; Genomic_DNA.
EMBL; D63464; BAA22982.1; -; Genomic_DNA.
EMBL; AF110456; AAF23554.1; -; Genomic_DNA.
EMBL; AB048394; BAB32568.1; -; Genomic_DNA.
EMBL; AB048395; BAB32569.1; -; Genomic_DNA.
EMBL; AY536888; AAS45601.2; -; Genomic_DNA.
EMBL; AC002291; AAC00625.1; -; Genomic_DNA.
EMBL; CP002684; AEE35937.1; -; Genomic_DNA.
EMBL; AY045612; AAK73970.1; -; mRNA.
EMBL; AY090330; AAL90991.1; -; mRNA.
EMBL; AY088010; AAM65556.1; -; mRNA.
EMBL; AF056557; AAD41572.1; -; Genomic_DNA.
PIR; A23815; DEMUAM.
RefSeq; NP_177837.1; NM_106362.3.
UniGene; At.22653; -.
UniGene; At.64099; -.
PDB; 4RQT; X-ray; 2.30 A; A=6-379.
PDB; 4RQU; X-ray; 2.50 A; A/B=6-379.
PDBsum; 4RQT; -.
PDBsum; 4RQU; -.
ProteinModelPortal; P06525; -.
SMR; P06525; -.
BioGrid; 29266; 2.
STRING; 3702.AT1G77120.1; -.
iPTMnet; P06525; -.
PaxDb; P06525; -.
PRIDE; P06525; -.
EnsemblPlants; AT1G77120.1; AT1G77120.1; AT1G77120.
GeneID; 844047; -.
Gramene; AT1G77120.1; AT1G77120.1; AT1G77120.
KEGG; ath:AT1G77120; -.
Araport; AT1G77120; -.
TAIR; locus:2025237; AT1G77120.
eggNOG; KOG0022; Eukaryota.
eggNOG; COG1062; LUCA.
InParanoid; P06525; -.
KO; K18857; -.
OMA; GACRIIG; -.
OrthoDB; EOG09360BVQ; -.
PhylomeDB; P06525; -.
PRO; PR:P06525; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; P06525; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:TAIR.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IMP:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0031000; P:response to caffeine; IEP:UniProtKB.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEP:UniProtKB.
GO; GO:0009413; P:response to flooding; IEP:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IGI:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SUPFAM; SSF50129; SSF50129; 2.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Glutathionylation; Metal-binding; NAD; Nucleotide-binding;
Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 379 Alcohol dehydrogenase class-P.
/FTId=PRO_0000160697.
NP_BIND 202 207 NAD. {ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
NP_BIND 295 297 NAD. {ECO:0000250|UniProtKB:P00327}.
METAL 47 47 Zinc 1; catalytic. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 49 49 Zinc 1. {ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 69 69 Zinc 1; catalytic. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 99 99 Zinc 2. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 102 102 Zinc 2. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 105 105 Zinc 2. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 113 113 Zinc 2. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
METAL 177 177 Zinc 1; catalytic. {ECO:0000244|PDB:4RQT,
ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 49 49 NAD. {ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 49 49 Substrate. {ECO:0000244|PDB:4RQT,
ECO:0000269|PubMed:25447145}.
BINDING 69 69 Substrate.
{ECO:0000250|UniProtKB:P00327}.
BINDING 226 226 NAD. {ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 231 231 NAD. {ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 272 272 NAD; via carbonyl oxygen.
{ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 295 295 NAD; via carbonyl oxygen.
{ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 322 322 NAD; via amide nitrogen.
{ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
BINDING 372 372 NAD. {ECO:0000244|PDB:4RQU,
ECO:0000269|PubMed:25447145}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19245862}.
VARIANT 43 43 F -> Y (in strain: cv. Hiroshima).
{ECO:0000269|PubMed:8587508}.
VARIANT 51 51 V -> L (in strain: cv. Bla-10, cv. Ci-0,
cv. Cvi-0, cv. Hiroshima, cv. Kas-1 and
cv. Ita-0). {ECO:0000269|PubMed:11158375,
ECO:0000269|PubMed:8587508,
ECO:0000269|PubMed:8844162}.
VARIANT 101 101 E -> D (in strain: cv. Aa-0, cv. Al-0,
cv. Bl-1, cv. Bs-0, cv. Gr-1, cv. Mt-0,
cv. Shokei and cv. Yo-0).
{ECO:0000269|PubMed:8587508,
ECO:0000269|PubMed:8844162,
ECO:0000269|Ref.11}.
VARIANT 106 106 H -> K (in strain: cv. Bl-1 and cv. Gr-
1). {ECO:0000269|PubMed:8844162,
ECO:0000269|Ref.11}.
VARIANT 106 106 H -> Q (in strain: cv. Aa-0, cv. Al-0,
cv. Bs-0, cv. Mt-0, cv. Shokei and cv.
Yo-0). {ECO:0000269|PubMed:8587508,
ECO:0000269|PubMed:8844162}.
VARIANT 120 120 T -> P (in strain: cv. Es-0).
{ECO:0000269|PubMed:8844162}.
VARIANT 180 180 S -> A (in strain: cv. Bla-10).
{ECO:0000269|PubMed:8844162}.
VARIANT 197 197 S -> T (in strain: cv. Cvi-0).
{ECO:0000269|PubMed:11158375}.
VARIANT 217 217 A -> V (in strain: cv. Kas-1).
{ECO:0000269|PubMed:11158375}.
MUTAGEN 105 105 C->Y: In R006; inactive enzyme.
{ECO:0000269|PubMed:2277648,
ECO:0000269|PubMed:3377754}.
CONFLICT 154 154 V -> L (in Ref. 11; AAM65556).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:4RQT}.
STRAND 23 29 {ECO:0000244|PDB:4RQT}.
STRAND 36 45 {ECO:0000244|PDB:4RQT}.
HELIX 48 54 {ECO:0000244|PDB:4RQT}.
STRAND 70 78 {ECO:0000244|PDB:4RQT}.
STRAND 90 93 {ECO:0000244|PDB:4RQT}.
STRAND 100 102 {ECO:0000244|PDB:4RQT}.
HELIX 103 106 {ECO:0000244|PDB:4RQT}.
STRAND 107 109 {ECO:0000244|PDB:4RQT}.
TURN 114 116 {ECO:0000244|PDB:4RQT}.
TURN 126 128 {ECO:0000244|PDB:4RQT}.
STRAND 132 135 {ECO:0000244|PDB:4RQT}.
STRAND 138 141 {ECO:0000244|PDB:4RQT}.
TURN 144 146 {ECO:0000244|PDB:4RQT}.
STRAND 149 156 {ECO:0000244|PDB:4RQT}.
HELIX 157 159 {ECO:0000244|PDB:4RQT}.
STRAND 160 162 {ECO:0000244|PDB:4RQT}.
HELIX 169 172 {ECO:0000244|PDB:4RQT}.
HELIX 173 176 {ECO:0000244|PDB:4RQT}.
HELIX 178 187 {ECO:0000244|PDB:4RQT}.
TURN 188 190 {ECO:0000244|PDB:4RQT}.
STRAND 197 201 {ECO:0000244|PDB:4RQT}.
HELIX 205 216 {ECO:0000244|PDB:4RQT}.
STRAND 220 225 {ECO:0000244|PDB:4RQT}.
HELIX 229 231 {ECO:0000244|PDB:4RQT}.
HELIX 232 235 {ECO:0000244|PDB:4RQT}.
HELIX 236 238 {ECO:0000244|PDB:4RQT}.
STRAND 242 244 {ECO:0000244|PDB:4RQT}.
HELIX 246 248 {ECO:0000244|PDB:4RQT}.
HELIX 253 260 {ECO:0000244|PDB:4RQT}.
STRAND 265 270 {ECO:0000244|PDB:4RQT}.
HELIX 275 283 {ECO:0000244|PDB:4RQT}.
TURN 287 289 {ECO:0000244|PDB:4RQT}.
STRAND 291 294 {ECO:0000244|PDB:4RQT}.
HELIX 309 312 {ECO:0000244|PDB:4RQT}.
STRAND 316 319 {ECO:0000244|PDB:4RQT}.
HELIX 322 324 {ECO:0000244|PDB:4RQT}.
HELIX 327 339 {ECO:0000244|PDB:4RQT}.
HELIX 346 348 {ECO:0000244|PDB:4RQT}.
STRAND 349 354 {ECO:0000244|PDB:4RQT}.
HELIX 355 358 {ECO:0000244|PDB:4RQT}.
HELIX 359 366 {ECO:0000244|PDB:4RQT}.
STRAND 371 376 {ECO:0000244|PDB:4RQT}.
SEQUENCE 379 AA; 41178 MW; 32550529538B9669 CRC64;
MSTTGQIIRC KAAVAWEAGK PLVIEEVEVA PPQKHEVRIK ILFTSLCHTD VYFWEAKGQT
PLFPRIFGHE AGGIVESVGE GVTDLQPGDH VLPIFTGECG ECRHCHSEES NMCDLLRINT
ERGGMIHDGE SRFSINGKPI YHFLGTSTFS EYTVVHSGQV AKINPDAPLD KVCIVSCGLS
TGLGATLNVA KPKKGQSVAI FGLGAVGLGA AEGARIAGAS RIIGVDFNSK RFDQAKEFGV
TECVNPKDHD KPIQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK
DDAFKTHPMN FLNERTLKGT FFGNYKPKTD IPGVVEKYMN KELELEKFIT HTVPFSEINK
AFDYMLKGES IRCIITMGA


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