UniProtKB - P06525 (ADH1_ARATH)
Protein
Alcohol dehydrogenase class-P
Gene
ADH1
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Functioni
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).4 Publications
Miscellaneous
Unlike most plants, Arabidopsis contains only one gene for ADH.1 Publication
Catalytic activityi
Cofactori
Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication
Activity regulationi
Alcohol dehydrogenase activity show inverse correlation with the decreasing availability of oxygen.1 Publication
Kineticsi
kcat is 328 min(-1) with NAD+ as substrate (at pH 10.5 and 25 degrees Celsius).1 Publication
- KM=1.65 mM for NAD+ (at pH 10.5 and 25 degrees Celsius)1 Publication
- KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius)1 Publication
- Vmax=7.9 µmol/min/mg enzyme with NAD+ as substrate (at pH 10.5 and 25 degrees Celsius)1 Publication
- Vmax=70.1 µmol/min/mg enzyme with ethanol as substrate (at pH 10.5 and 25 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 10.5 (at 25 degrees Celsius).1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 47 | Zinc 1; catalyticCombined sources1 Publication | 1 | |
Metal bindingi | 49 | Zinc 1Combined sources1 Publication | 1 | |
Binding sitei | 49 | NADCombined sources1 Publication | 1 | |
Binding sitei | 49 | SubstrateCombined sources1 Publication | 1 | |
Metal bindingi | 69 | Zinc 1; catalyticCombined sources1 Publication | 1 | |
Binding sitei | 69 | SubstrateBy similarity | 1 | |
Metal bindingi | 99 | Zinc 2Combined sources1 Publication | 1 | |
Metal bindingi | 102 | Zinc 2Combined sources1 Publication | 1 | |
Metal bindingi | 105 | Zinc 2Combined sources1 Publication | 1 | |
Metal bindingi | 113 | Zinc 2Combined sources1 Publication | 1 | |
Metal bindingi | 177 | Zinc 1; catalyticCombined sources1 Publication | 1 | |
Binding sitei | 226 | NADCombined sources1 Publication | 1 | |
Binding sitei | 231 | NADCombined sources1 Publication | 1 | |
Binding sitei | 272 | NAD; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 295 | NAD; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 322 | NAD; via amide nitrogenCombined sources1 Publication | 1 | |
Binding sitei | 372 | NADCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 202 – 207 | NADCombined sources1 Publication | 6 | |
Nucleotide bindingi | 295 – 297 | NADBy similarity | 3 |
GO - Molecular functioni
- alcohol dehydrogenase (NAD+) activity Source: TAIR
- alcohol dehydrogenase activity, zinc-dependent Source: GO_Central
- nucleotide binding Source: UniProtKB-KW
- protein homodimerization activity Source: UniProtKB
- S-(hydroxymethyl)glutathione dehydrogenase activity Source: GO_Central
- zinc ion binding Source: GO_Central
GO - Biological processi
- cellular response to hypoxia Source: TAIR
- formaldehyde catabolic process Source: GO_Central
- positive regulation of cellular response to hypoxia Source: UniProtKB
- response to abscisic acid Source: UniProtKB
- response to cadmium ion Source: TAIR
- response to caffeine Source: UniProtKB
- response to cold Source: UniProtKB
- response to estradiol Source: UniProtKB
- response to flooding Source: UniProtKB
- response to hydrogen peroxide Source: UniProtKB
- response to hypoxia Source: UniProtKB
- response to osmotic stress Source: TAIR
- response to salt stress Source: UniProtKB
- response to sucrose Source: UniProtKB
- response to water deprivation Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Metal-binding, NAD, Nucleotide-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: Alcohol dehydrogenase class-PCurated (EC:1.1.1.12 Publications)Short name: AtADH1 Publication |
Gene namesi | Name:ADH11 Publication Synonyms:ADH1 Publication Ordered Locus Names:At1g77120Imported ORF Names:F22K20.19Imported |
Organismi | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic identifieri | 3702 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Proteomesi |
|
Organism-specific databases
Araporti | AT1G77120 |
TAIRi | locus:2025237, AT1G77120 |
Subcellular locationi
Other locations
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: TAIR
Plasma Membrane
- plasma membrane Source: TAIR
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
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).5 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 105 | C → Y in R006; inactive enzyme. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000160697 | 2 – 379 | Alcohol dehydrogenase class-PAdd BLAST | 378 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 229 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Glutathionylated.1 Publication
Keywords - PTMi
Acetylation, Glutathionylation, PhosphoproteinProteomic databases
PaxDbi | P06525 |
PRIDEi | P06525 |
ProteomicsDBi | 244713 |
PTM databases
iPTMneti | P06525 |
MetOSitei | P06525 |
Expressioni
Tissue specificityi
Root specific (PubMed:9611167). Also detected in etiolated seedlings and leaves in cold conditons (PubMed:12231733).2 Publications
Inductioni
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 H2O2 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).1 Publication11 Publications
Gene expression databases
ExpressionAtlasi | P06525, baseline and differential |
Genevisiblei | P06525, AT |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 29266, 2 interactors |
STRINGi | 3702.AT1G77120.1 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P06525 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0022, Eukaryota |
HOGENOMi | CLU_026673_14_0_1 |
InParanoidi | P06525 |
OMAi | GEVIRCK |
OrthoDBi | 664798at2759 |
PhylomeDBi | P06525 |
Family and domain databases
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR002328, ADH_Zn_CS IPR011032, GroES-like_sf IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF00107, ADH_zinc_N, 1 hit |
SUPFAMi | SSF50129, SSF50129, 2 hits SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P06525-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTTGQIIRC KAAVAWEAGK PLVIEEVEVA PPQKHEVRIK ILFTSLCHTD
60 70 80 90 100
VYFWEAKGQT PLFPRIFGHE AGGIVESVGE GVTDLQPGDH VLPIFTGECG
110 120 130 140 150
ECRHCHSEES NMCDLLRINT ERGGMIHDGE SRFSINGKPI YHFLGTSTFS
160 170 180 190 200
EYTVVHSGQV AKINPDAPLD KVCIVSCGLS TGLGATLNVA KPKKGQSVAI
210 220 230 240 250
FGLGAVGLGA AEGARIAGAS RIIGVDFNSK RFDQAKEFGV TECVNPKDHD
260 270 280 290 300
KPIQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK
310 320 330 340 350
DDAFKTHPMN FLNERTLKGT FFGNYKPKTD IPGVVEKYMN KELELEKFIT
360 370
HTVPFSEINK AFDYMLKGES IRCIITMGA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 154 | V → L in AAM65556 (Ref. 11) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 43 | F → Y in strain: cv. Hiroshima. 1 Publication | 1 | |
Natural varianti | 51 | V → L in strain: cv. Bla-10, cv. Ci-0, cv. Cvi-0, cv. Hiroshima, cv. Kas-1 and cv. Ita-0. 3 Publications | 1 | |
Natural varianti | 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. 3 Publications | 1 | |
Natural varianti | 106 | H → K in strain: cv. Bl-1 and cv. Gr-1. 2 Publications | 1 | |
Natural varianti | 106 | H → Q in strain: cv. Aa-0, cv. Al-0, cv. Bs-0, cv. Mt-0, cv. Shokei and cv. Yo-0. 2 Publications | 1 | |
Natural varianti | 120 | T → P in strain: cv. Es-0. 1 Publication | 1 | |
Natural varianti | 180 | S → A in strain: cv. Bla-10. 1 Publication | 1 | |
Natural varianti | 197 | S → T in strain: cv. Cvi-0. 1 Publication | 1 | |
Natural varianti | 217 | A → V in strain: cv. Kas-1. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M12196 Genomic DNA Translation: AAA32728.1 X77943 Genomic DNA Translation: CAA54911.1 D84240 Genomic DNA Translation: BAA19615.1 D84241 Genomic DNA Translation: BAA19616.1 D84242 Genomic DNA Translation: BAA19617.1 D84243 Genomic DNA Translation: BAA19618.1 D84244 Genomic DNA Translation: BAA19619.1 D84245 Genomic DNA Translation: BAA19620.1 D84246 Genomic DNA Translation: BAA19621.1 D84247 Genomic DNA Translation: BAA19622.1 D84248 Genomic DNA Translation: BAA19623.1 D84249 Genomic DNA Translation: BAA19624.1 D63460 Genomic DNA Translation: BAA22983.1 D63461 Genomic DNA Translation: BAA22979.1 D63462 Genomic DNA Translation: BAA22980.1 D63463 Genomic DNA Translation: BAA22981.1 D63464 Genomic DNA Translation: BAA22982.1 AF110456 Genomic DNA Translation: AAF23554.1 AB048394 Genomic DNA Translation: BAB32568.1 AB048395 Genomic DNA Translation: BAB32569.1 AY536888 Genomic DNA Translation: AAS45601.2 AC002291 Genomic DNA Translation: AAC00625.1 CP002684 Genomic DNA Translation: AEE35937.1 AY045612 mRNA Translation: AAK73970.1 AY090330 mRNA Translation: AAL90991.1 AY088010 mRNA Translation: AAM65556.1 AF056557 Genomic DNA Translation: AAD41572.1 |
PIRi | A23815, DEMUAM |
RefSeqi | NP_177837.1, NM_106362.3 |
Genome annotation databases
EnsemblPlantsi | AT1G77120.1; AT1G77120.1; AT1G77120 |
GeneIDi | 844047 |
Gramenei | AT1G77120.1; AT1G77120.1; AT1G77120 |
KEGGi | ath:AT1G77120 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M12196 Genomic DNA Translation: AAA32728.1 X77943 Genomic DNA Translation: CAA54911.1 D84240 Genomic DNA Translation: BAA19615.1 D84241 Genomic DNA Translation: BAA19616.1 D84242 Genomic DNA Translation: BAA19617.1 D84243 Genomic DNA Translation: BAA19618.1 D84244 Genomic DNA Translation: BAA19619.1 D84245 Genomic DNA Translation: BAA19620.1 D84246 Genomic DNA Translation: BAA19621.1 D84247 Genomic DNA Translation: BAA19622.1 D84248 Genomic DNA Translation: BAA19623.1 D84249 Genomic DNA Translation: BAA19624.1 D63460 Genomic DNA Translation: BAA22983.1 D63461 Genomic DNA Translation: BAA22979.1 D63462 Genomic DNA Translation: BAA22980.1 D63463 Genomic DNA Translation: BAA22981.1 D63464 Genomic DNA Translation: BAA22982.1 AF110456 Genomic DNA Translation: AAF23554.1 AB048394 Genomic DNA Translation: BAB32568.1 AB048395 Genomic DNA Translation: BAB32569.1 AY536888 Genomic DNA Translation: AAS45601.2 AC002291 Genomic DNA Translation: AAC00625.1 CP002684 Genomic DNA Translation: AEE35937.1 AY045612 mRNA Translation: AAK73970.1 AY090330 mRNA Translation: AAL90991.1 AY088010 mRNA Translation: AAM65556.1 AF056557 Genomic DNA Translation: AAD41572.1 |
PIRi | A23815, DEMUAM |
RefSeqi | NP_177837.1, NM_106362.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4RQT | X-ray | 2.30 | A | 6-379 | [»] | |
4RQU | X-ray | 2.50 | A/B | 6-379 | [»] | |
SMRi | P06525 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 29266, 2 interactors |
STRINGi | 3702.AT1G77120.1 |
PTM databases
iPTMneti | P06525 |
MetOSitei | P06525 |
Proteomic databases
PaxDbi | P06525 |
PRIDEi | P06525 |
ProteomicsDBi | 244713 |
Genome annotation databases
EnsemblPlantsi | AT1G77120.1; AT1G77120.1; AT1G77120 |
GeneIDi | 844047 |
Gramenei | AT1G77120.1; AT1G77120.1; AT1G77120 |
KEGGi | ath:AT1G77120 |
Organism-specific databases
Araporti | AT1G77120 |
TAIRi | locus:2025237, AT1G77120 |
Phylogenomic databases
eggNOGi | KOG0022, Eukaryota |
HOGENOMi | CLU_026673_14_0_1 |
InParanoidi | P06525 |
OMAi | GEVIRCK |
OrthoDBi | 664798at2759 |
PhylomeDBi | P06525 |
Miscellaneous databases
PROi | PR:P06525 |
Gene expression databases
ExpressionAtlasi | P06525, baseline and differential |
Genevisiblei | P06525, AT |
Family and domain databases
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR002328, ADH_Zn_CS IPR011032, GroES-like_sf IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF00107, ADH_zinc_N, 1 hit |
SUPFAMi | SSF50129, SSF50129, 2 hits SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ADH1_ARATH | |
Accessioni | P06525Primary (citable) accession number: P06525 Secondary accession number(s): O04080 Q9SX08 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | May 29, 2007 | |
Last modified: | December 2, 2020 | |
This is version 180 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Arabidopsis thaliana
Arabidopsis thaliana: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families