ADH1_ARATH
ID ADH1_ARATH Reviewed; 379 AA.
AC P06525; O04080; O04713; O04717; O04868; O23821; Q8LA61; Q94AY6; Q9CAZ2;
AC Q9CAZ3; Q9SX08;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Alcohol dehydrogenase class-P {ECO:0000305};
DE Short=AtADH {ECO:0000303|PubMed:25447145};
DE EC=1.1.1.1 {ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754};
GN Name=ADH1 {ECO:0000303|PubMed:3377754};
GN Synonyms=ADH {ECO:0000303|PubMed:2937058};
GN OrderedLocusNames=At1g77120 {ECO:0000312|Araport:AT1G77120};
GN ORFNames=F22K20.19 {ECO:0000312|EMBL:AAC00625.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY
RP 2,4-DICHLOROPHENOXYACETIC ACID.
RX PubMed=2937058; DOI=10.1073/pnas.83.5.1408;
RA Chang C., Meyerowitz E.M.;
RT "Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol
RT dehydrogenase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1408-1412(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=7851777; DOI=10.1093/genetics/138.3.811;
RA Hanfstingl U., Berry A., Kellogg E.A., Costa J.T. III, Ruediger W.,
RA Ausubel F.M.;
RT "Haplotypic divergence coupled with lack of diversity at the Arabidopsis
RT thaliana alcohol dehydrogenase locus: roles for both balancing and
RT directional selection?";
RL Genetics 138:811-828(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Al-0, cv. Bl-1, cv. Bla-10, cv. Bs-0, cv. Chi-0, cv. Ci-0,
RC cv. Es-0, cv. Gr-1, cv. Ita-0, and cv. Yo-0;
RX PubMed=8844162; DOI=10.1093/genetics/143.4.1761;
RA Innan H., Tajima F., Terauchi R., Miyashita N.T.;
RT "Intragenic recombination in the Adh locus of the wild plant Arabidopsis
RT thaliana.";
RL Genetics 143:1761-1770(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Aa-0, cv. Hiroshima, cv. Mt-0, cv. Pog-0, and cv. Shokei;
RX PubMed=8587508; DOI=10.1093/oxfordjournals.molbev.a025603;
RA Miyashita N.T., Innan H., Terauchi R.;
RT "Intra- and interspecific variation of the alcohol dehydrogenase locus
RT region in wild plants Arabis gemmifera and Arabidopsis thaliana.";
RL Mol. Biol. Evol. 13:433-436(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11018155; DOI=10.1093/oxfordjournals.molbev.a026248;
RA Koch M.A., Haubold B., Mitchell-Olds T.;
RT "Comparative evolutionary analysis of chalcone synthase and alcohol
RT dehydrogenase loci in Arabidopsis, Arabis, and related genera
RT (Brassicaceae).";
RL Mol. Biol. Evol. 17:1483-1498(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Cvi-0, and cv. Kas-1;
RX PubMed=11158375; DOI=10.1093/oxfordjournals.molbev.a003790;
RA Miyashita N.T.;
RT "DNA variation in the 5' upstream region of the Adh locus of the wild
RT plants Arabidopsis thaliana and Arabis gemmifera.";
RL Mol. Biol. Evol. 18:164-171(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. C24;
RA Santos D.;
RT "Post-transcriptional silencing of the Arabidopsis adh1 gene triggered by a
RT fully homologous transgene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [9]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-101 AND LYS-106.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-331.
RC STRAIN=cv. Columbia;
RX PubMed=10382288; DOI=10.1139/gen-42-3-387;
RA Brunel D., Froger N., Pelletier G.;
RT "Development of amplified consensus genetic markers (ACGM) in Brassica
RT napus from Arabidopsis thaliana sequences of known biological function.";
RL Genome 42:387-402(1999).
RN [13]
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-105, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Be-0, and cv. Ts-1;
RX PubMed=3377754; DOI=10.1007/bf00555492;
RA Jacobs M., Dolferus R., Van den Bossche D.;
RT "Isolation and biochemical analysis of ethyl methanesulfonate-induced
RT alcohol dehydrogenase null mutants of arabidopsis thaliana (L.) Heynh.";
RL Biochem. Genet. 26:105-122(1988).
RN [14]
RP MUTAGENESIS OF CYS-105.
RC STRAIN=cv. Be-0;
RX PubMed=2277648; DOI=10.1007/bf00271565;
RA Dolferus R., van den Bossche D., Jacobs M.;
RT "Sequence analysis of two null-mutant alleles of the single Arabidopsis Adh
RT locus.";
RL Mol. Gen. Genet. 224:297-302(1990).
RN [15]
RP INDUCTION BY COLD.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12231733; DOI=10.1104/pp.101.3.833;
RA Jarillo J.A., Leyva A., Salinas J., Martinez-Zapater J.M.;
RT "Low temperature induces the accumulation of alcohol dehydrogenase mRNA in
RT Arabidopsis thaliana, a chilling-tolerant plant.";
RL Plant Physiol. 101:833-837(1993).
RN [16]
RP INDUCTION BY HYPOXIA; ABSCISIC ACID; DEHYDRATION AND COLD.
RC STRAIN=cv. C24;
RX PubMed=8787023; DOI=10.1104/pp.111.2.381;
RA de Bruxelles G.L., Peacock W.J., Dennis E.S., Dolferus R.;
RT "Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis.";
RL Plant Physiol. 111:381-391(1996).
RN [17]
RP ACTIVITY REGULATION, AND INDUCTION BY HYPOXIA.
RX PubMed=9522467; DOI=10.1093/oxfordjournals.pcp.a029129;
RA Porterfield D.M., Crispi M.L., Musgrave M.E.;
RT "Changes in soluble sugar, starch, and alcohol dehydrogenase in Arabidopsis
RT thaliana exposed to N2 diluted atmospheres.";
RL Plant Cell Physiol. 38:1354-1358(1997).
RN [18]
RP INDUCTION BY MYB2; ABSCISIC ACID; DEHYDRATION; COLD AND HYPOXIA, AND TISSUE
RP SPECIFICITY.
RX PubMed=9611167; DOI=10.1093/genetics/149.2.479;
RA Hoeren F.U., Dolferus R., Wu Y., Peacock W.J., Dennis E.S.;
RT "Evidence for a role for AtMYB2 in the induction of the Arabidopsis alcohol
RT dehydrogenase gene (ADH1) by low oxygen.";
RL Genetics 149:479-490(1998).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=9880346; DOI=10.1104/pp.119.1.57;
RA Ellis M.H., Dennis E.S., Peacock W.J.;
RT "Arabidopsis roots and shoots have different mechanisms for hypoxic stress
RT tolerance.";
RL Plant Physiol. 119:57-64(1999).
RN [20]
RP INDUCTION BY SPACEFLIGHT AND HYPOXIA.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11402191; DOI=10.1104/pp.126.2.613;
RA Paul A.-L., Daugherty C.J., Bihn E.A., Chapman D.K., Norwood K.L.L.,
RA Ferl R.J.;
RT "Transgene expression patterns indicate that spaceflight affects stress
RT signal perception and transduction in arabidopsis.";
RL Plant Physiol. 126:613-621(2001).
RN [21]
RP INDUCTION BY HYPOXIA.
RX PubMed=11402202; DOI=10.1104/pp.126.2.742;
RA Peng H.P., Chan C.S., Shih M.C., Yang S.F.;
RT "Signaling events in the hypoxic induction of alcohol dehydrogenase gene in
RT Arabidopsis.";
RL Plant Physiol. 126:742-749(2001).
RN [22]
RP INDUCTION BY HYPOXIA, HIGH SALT, COLD, AND ABCISSIC ACID.
RX PubMed=11987307;
RA Manak M.S., Paul A.L., Sehnke P.C., Ferl R.J.;
RT "Remote sensing of gene expression in Planta: transgenic plants as monitors
RT of exogenous stress perception in extraterrestrial environments.";
RL Life Support Biosph. Sci. 8:83-91(2002).
RN [23]
RP INDUCTION BY OXYGEN DEPRIVATION AND CAFFEINE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12509334; DOI=10.1093/aob/mcf119;
RA Baxter-Burrell A., Chang R., Springer P., Bailey-Serres J.;
RT "Gene and enhancer trap transposable elements reveal oxygen deprivation-
RT regulated genes and their complex patterns of expression in Arabidopsis.";
RL Ann. Bot. 91:129-141(2003).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=12857811; DOI=10.1104/pp.103.022244;
RA Ismond K.P., Dolferus R., de Pauw M., Dennis E.S., Good A.G.;
RT "Enhanced low oxygen survival in Arabidopsis through increased metabolic
RT flux in the fermentative pathway.";
RL Plant Physiol. 132:1292-1302(2003).
RN [25]
RP GLUTATHIONYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=16055689; DOI=10.1104/pp.104.058917;
RA Dixon D.P., Skipsey M., Grundy N.M., Edwards R.;
RT "Stress-induced protein S-glutathionylation in Arabidopsis.";
RL Plant Physiol. 138:2233-2244(2005).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [27]
RP INDUCTION BY ABSCISIC ACID; ESTRADIOL; NACL; H2O2 AND SUCROSE.
RX PubMed=18441225; DOI=10.1104/pp.108.116897;
RA Papdi C., Abraham E., Joseph M.P., Popescu C., Koncz C., Szabados L.;
RT "Functional identification of Arabidopsis stress regulatory genes using the
RT controlled cDNA overexpression system.";
RL Plant Physiol. 147:528-542(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [29]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20508152; DOI=10.1073/pnas.0914991107;
RA Zhang F., Maeder M.L., Unger-Wallace E., Hoshaw J.P., Reyon D.,
RA Christian M., Li X., Pierick C.J., Dobbs D., Peterson T., Joung J.K.,
RA Voytas D.F.;
RT "High frequency targeted mutagenesis in Arabidopsis thaliana using zinc
RT finger nucleases.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12028-12033(2010).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [31]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMER, AND CATALYTIC ACTIVITY.
RX PubMed=23707506; DOI=10.1016/j.pep.2013.05.004;
RA Cheng F., Hu T., An Y., Huang J., Xu Y.;
RT "Purification and enzymatic characterization of alcohol dehydrogenase from
RT Arabidopsis thaliana.";
RL Protein Expr. Purif. 90:74-77(2013).
RN [32]
RP INDUCTION BY HYDROGEN PEROXIDE.
RC STRAIN=cv. Columbia;
RX PubMed=24395201; DOI=10.1007/s00425-013-2020-z;
RA Yang C.-Y.;
RT "Hydrogen peroxide controls transcriptional responses of ERF73/HRE1 and
RT ADH1 via modulation of ethylene signaling during hypoxic stress.";
RL Planta 239:877-885(2014).
RN [33]
RP INDUCTION BY WATER SUBMERGENCE.
RX PubMed=26566261; DOI=10.1080/15548627.2015.1112483;
RA Chen L., Liao B., Qi H., Xie L.J., Huang L., Tan W.J., Zhai N., Yuan L.B.,
RA Zhou Y., Yu L.J., Chen Q.F., Shu W., Xiao S.;
RT "Autophagy contributes to regulation of the hypoxia response during
RT submergence in Arabidopsis thaliana.";
RL Autophagy 11:2233-2246(2015).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 6-379 IN COMPLEX WITH NAD;
RP SUBSTRATE AND ZINC, COFACTOR, AND HOMODIMER.
RX PubMed=25447145; DOI=10.1016/j.biochi.2014.10.023;
RA Chen F., Wang P., An Y., Huang J., Xu Y.;
RT "Structural insight into the conformational change of alcohol dehydrogenase
RT from Arabidopsis thaliana L. during coenzyme binding.";
RL Biochimie 108:33-39(2015).
CC -!- FUNCTION: Alcohol dehydrogenase mostly active on ethanol (EtOH), but
CC exhibits broad substrates selectivity for primary and secondary
CC alcohols (e.g. butanol, propyl alcohol, pentanol, isopentanol, ethylene
CC glycol, isopropanol, methanol and tertiary butyl alcohol)
CC (PubMed:23707506). Converts allyl alcohol to highly toxic acryl-
CC aldehyde (PubMed:20508152). Required for survival and acclimation in
CC hypoxic conditions, especially in roots (PubMed:12857811,
CC PubMed:9880346). {ECO:0000269|PubMed:12857811,
CC ECO:0000269|PubMed:20508152, ECO:0000269|PubMed:23707506,
CC ECO:0000269|PubMed:9880346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:25447145};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:25447145};
CC -!- ACTIVITY REGULATION: Alcohol dehydrogenase activity show inverse
CC correlation with the decreasing availability of oxygen.
CC {ECO:0000269|PubMed:9522467}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.65 mM for NAD(+) (at pH 10.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23707506};
CC KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23707506};
CC Vmax=7.9 umol/min/mg enzyme with NAD(+) as substrate (at pH 10.5 and
CC 25 degrees Celsius) {ECO:0000269|PubMed:23707506};
CC Vmax=70.1 umol/min/mg enzyme with ethanol as substrate (at pH 10.5
CC and 25 degrees Celsius) {ECO:0000269|PubMed:23707506};
CC Note=kcat is 328 min(-1) with NAD(+) as substrate (at pH 10.5 and 25
CC degrees Celsius). {ECO:0000269|PubMed:23707506};
CC pH dependence:
CC Optimum pH is 10.5 (at 25 degrees Celsius).
CC {ECO:0000269|PubMed:23707506};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23707506,
CC ECO:0000269|PubMed:25447145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7851777}.
CC -!- TISSUE SPECIFICITY: Root specific (PubMed:9611167). Also detected in
CC etiolated seedlings and leaves in cold conditons (PubMed:12231733).
CC {ECO:0000269|PubMed:12231733, ECO:0000269|PubMed:9611167}.
CC -!- INDUCTION: Transactivated by MYB2 in response to various stresses
CC (PubMed:9611167). By 2,4-dichlorophenoxyacetic acid (synthetic auxin)
CC in Arabidopsis as well as in maize (PubMed:2937058). Induced mostly in
CC roots and shoot apex by hypoxia during water submergence or oxygen
CC deprivation, in a MYB2-dependent manner, and partly via an ethylene-
CC mediated pathway (PubMed:9522467, PubMed:9611167, PubMed:11402202,
CC PubMed:12509334, PubMed:26566261, PubMed:11987307, PubMed:8787023).
CC Accumulates in response to hydrogen peroxide H(2)O(2) during the early
CC stages of hypoxia signaling (PubMed:24395201, PubMed:18441225).
CC Decreased levels upon combined hypoxia and diphenylene iodonium
CC chloride (DPI, an NADPH oxidase inhibitor) treatments
CC (PubMed:24395201). Induced by abscisic acid (ABA), dehydration,
CC estradiol, salt (NaCl), cold and sucrose treatments (PubMed:12231733,
CC PubMed:18441225, PubMed:11987307, PubMed:9611167, PubMed:8787023). The
CC induction by dehydration is ABA-dependent (PubMed:8787023). Observed in
CC etiolated seedlings and leaves upon exposure to low temperature,
CC probably via anaerobic metabolism and increase of ABA levels
CC (PubMed:12231733). Strongly induced by caffeine (PubMed:12509334). May
CC accumulate in roots during spaceflight, probably due to local hypoxia
CC conditions (PubMed:11402191). {ECO:0000269|PubMed:11402191,
CC ECO:0000269|PubMed:11402202, ECO:0000269|PubMed:11987307,
CC ECO:0000269|PubMed:12231733, ECO:0000269|PubMed:12509334,
CC ECO:0000269|PubMed:18441225, ECO:0000269|PubMed:24395201,
CC ECO:0000269|PubMed:26566261, ECO:0000269|PubMed:8787023,
CC ECO:0000269|PubMed:9522467, ECO:0000269|PubMed:9611167,
CC ECO:0000303|PubMed:2937058}.
CC -!- PTM: Glutathionylated. {ECO:0000269|PubMed:16055689}.
CC -!- DISRUPTION PHENOTYPE: Loss of alcohol dehydrogenase activity
CC (PubMed:3377754, PubMed:12509334). Increased resistance to allyl
CC alcohol (PubMed:20508152). Decreased survival, associated with impaired
CC lateral roots development, upon oxygen deprivation leading to hypoxic
CC conditions (PubMed:12509334, PubMed:12857811). Impaired root
CC acclimation to hypoxic stress (PubMed:9880346).
CC {ECO:0000269|PubMed:12509334, ECO:0000269|PubMed:12857811,
CC ECO:0000269|PubMed:20508152, ECO:0000269|PubMed:3377754,
CC ECO:0000269|PubMed:9880346}.
CC -!- MISCELLANEOUS: Unlike most plants, Arabidopsis contains only one gene
CC for ADH. {ECO:0000303|PubMed:3377754}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-P subfamily. {ECO:0000305}.
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DR EMBL; M12196; AAA32728.1; -; Genomic_DNA.
DR EMBL; X77943; CAA54911.1; -; Genomic_DNA.
DR EMBL; D84240; BAA19615.1; -; Genomic_DNA.
DR EMBL; D84241; BAA19616.1; -; Genomic_DNA.
DR EMBL; D84242; BAA19617.1; -; Genomic_DNA.
DR EMBL; D84243; BAA19618.1; -; Genomic_DNA.
DR EMBL; D84244; BAA19619.1; -; Genomic_DNA.
DR EMBL; D84245; BAA19620.1; -; Genomic_DNA.
DR EMBL; D84246; BAA19621.1; -; Genomic_DNA.
DR EMBL; D84247; BAA19622.1; -; Genomic_DNA.
DR EMBL; D84248; BAA19623.1; -; Genomic_DNA.
DR EMBL; D84249; BAA19624.1; -; Genomic_DNA.
DR EMBL; D63460; BAA22983.1; -; Genomic_DNA.
DR EMBL; D63461; BAA22979.1; -; Genomic_DNA.
DR EMBL; D63462; BAA22980.1; -; Genomic_DNA.
DR EMBL; D63463; BAA22981.1; -; Genomic_DNA.
DR EMBL; D63464; BAA22982.1; -; Genomic_DNA.
DR EMBL; AF110456; AAF23554.1; -; Genomic_DNA.
DR EMBL; AB048394; BAB32568.1; -; Genomic_DNA.
DR EMBL; AB048395; BAB32569.1; -; Genomic_DNA.
DR EMBL; AY536888; AAS45601.2; -; Genomic_DNA.
DR EMBL; AC002291; AAC00625.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35937.1; -; Genomic_DNA.
DR EMBL; AY045612; AAK73970.1; -; mRNA.
DR EMBL; AY090330; AAL90991.1; -; mRNA.
DR EMBL; AY088010; AAM65556.1; -; mRNA.
DR EMBL; AF056557; AAD41572.1; -; Genomic_DNA.
DR PIR; A23815; DEMUAM.
DR RefSeq; NP_177837.1; NM_106362.3.
DR PDB; 4RQT; X-ray; 2.30 A; A=6-379.
DR PDB; 4RQU; X-ray; 2.50 A; A/B=6-379.
DR PDBsum; 4RQT; -.
DR PDBsum; 4RQU; -.
DR AlphaFoldDB; P06525; -.
DR SMR; P06525; -.
DR BioGRID; 29266; 4.
DR STRING; 3702.AT1G77120.1; -.
DR iPTMnet; P06525; -.
DR MetOSite; P06525; -.
DR PaxDb; P06525; -.
DR PRIDE; P06525; -.
DR ProteomicsDB; 244713; -.
DR EnsemblPlants; AT1G77120.1; AT1G77120.1; AT1G77120.
DR GeneID; 844047; -.
DR Gramene; AT1G77120.1; AT1G77120.1; AT1G77120.
DR KEGG; ath:AT1G77120; -.
DR Araport; AT1G77120; -.
DR TAIR; locus:2025237; AT1G77120.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P06525; -.
DR OMA; CANGQQY; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P06525; -.
DR BRENDA; 1.1.1.1; 399.
DR PRO; PR:P06525; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P06525; baseline and differential.
DR Genevisible; P06525; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:TAIR.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0031000; P:response to caffeine; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEP:UniProtKB.
DR GO; GO:0009413; P:response to flooding; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IGI:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Glutathionylation; Metal-binding;
KW NAD; Nucleotide-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..379
FT /note="Alcohol dehydrogenase class-P"
FT /id="PRO_0000160697"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU"
FT BINDING 202..207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 295..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT BINDING 372
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:25447145,
FT ECO:0007744|PDB:4RQU"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT VARIANT 43
FT /note="F -> Y (in strain: cv. Hiroshima)"
FT /evidence="ECO:0000269|PubMed:8587508"
FT VARIANT 51
FT /note="V -> L (in strain: cv. Bla-10, cv. Ci-0, cv. Cvi-0,
FT cv. Hiroshima, cv. Kas-1 and cv. Ita-0)"
FT /evidence="ECO:0000269|PubMed:11158375,
FT ECO:0000269|PubMed:8587508, ECO:0000269|PubMed:8844162"
FT VARIANT 101
FT /note="E -> D (in strain: cv. Aa-0, cv. Al-0, cv. Bl-1, cv.
FT Bs-0, cv. Gr-1, cv. Mt-0, cv. Shokei and cv. Yo-0)"
FT /evidence="ECO:0000269|PubMed:8587508,
FT ECO:0000269|PubMed:8844162, ECO:0000269|Ref.11"
FT VARIANT 106
FT /note="H -> K (in strain: cv. Bl-1 and cv. Gr-1)"
FT /evidence="ECO:0000269|PubMed:8844162, ECO:0000269|Ref.11"
FT VARIANT 106
FT /note="H -> Q (in strain: cv. Aa-0, cv. Al-0, cv. Bs-0, cv.
FT Mt-0, cv. Shokei and cv. Yo-0)"
FT /evidence="ECO:0000269|PubMed:8587508,
FT ECO:0000269|PubMed:8844162"
FT VARIANT 120
FT /note="T -> P (in strain: cv. Es-0)"
FT /evidence="ECO:0000269|PubMed:8844162"
FT VARIANT 180
FT /note="S -> A (in strain: cv. Bla-10)"
FT /evidence="ECO:0000269|PubMed:8844162"
FT VARIANT 197
FT /note="S -> T (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000269|PubMed:11158375"
FT VARIANT 217
FT /note="A -> V (in strain: cv. Kas-1)"
FT /evidence="ECO:0000269|PubMed:11158375"
FT MUTAGEN 105
FT /note="C->Y: In R006; inactive enzyme."
FT /evidence="ECO:0000269|PubMed:2277648,
FT ECO:0000269|PubMed:3377754"
FT CONFLICT 154
FT /note="V -> L (in Ref. 11; AAM65556)"
FT /evidence="ECO:0000305"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4RQT"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4RQT"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4RQT"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:4RQT"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4RQT"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:4RQT"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:4RQT"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:4RQT"
SQ 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
