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Protein

Alcohol dehydrogenase class-P

Gene

ADH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

A primary alcohol + NAD+ = an aldehyde + NADH.2 Publications
A secondary alcohol + NAD+ = a ketone + NADH.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Enzyme 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
  1. KM=1.65 mM for NAD+ (at pH 10.5 and 25 degrees Celsius)1 Publication
  2. KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius)1 Publication
  1. Vmax=7.9 µmol/min/mg enzyme with NAD+ as substrate (at pH 10.5 and 25 degrees Celsius)1 Publication
  2. 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Zinc 1; catalyticCombined sources1 Publication1
Metal bindingi49Zinc 1Combined sources1 Publication1
Binding sitei49NADCombined sources1 Publication1
Binding sitei49SubstrateCombined sources1 Publication1
Metal bindingi69Zinc 1; catalyticCombined sources1 Publication1
Binding sitei69SubstrateBy similarity1
Metal bindingi99Zinc 2Combined sources1 Publication1
Metal bindingi102Zinc 2Combined sources1 Publication1
Metal bindingi105Zinc 2Combined sources1 Publication1
Metal bindingi113Zinc 2Combined sources1 Publication1
Metal bindingi177Zinc 1; catalyticCombined sources1 Publication1
Binding sitei226NADCombined sources1 Publication1
Binding sitei231NADCombined sources1 Publication1
Binding sitei272NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei295NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei322NAD; via amide nitrogenCombined sources1 Publication1
Binding sitei372NADCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi202 – 207NADCombined sources1 Publication6
Nucleotide bindingi295 – 297NADBy similarity3

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: TAIR
  • nucleotide binding Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • 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 functionOxidoreductase
LigandMetal-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
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

AraportiAT1G77120.
TAIRilocus:2025237. AT1G77120.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & 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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105C → Y in R006; inactive enzyme. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001606972 – 379Alcohol dehydrogenase class-PAdd BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei229PhosphoserineCombined sources1

Post-translational modificationi

Glutathionylated.1 Publication

Keywords - PTMi

Acetylation, Glutathionylation, Phosphoprotein

Proteomic databases

PaxDbiP06525.
PRIDEiP06525.

PTM databases

iPTMnetiP06525.

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

GenevisibleiP06525. AT.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi29266. 2 interactors.
STRINGi3702.AT1G77120.1.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 15Combined sources8
Beta strandi23 – 29Combined sources7
Beta strandi36 – 45Combined sources10
Helixi48 – 54Combined sources7
Beta strandi70 – 78Combined sources9
Beta strandi90 – 93Combined sources4
Beta strandi100 – 102Combined sources3
Helixi103 – 106Combined sources4
Beta strandi107 – 109Combined sources3
Turni114 – 116Combined sources3
Turni126 – 128Combined sources3
Beta strandi132 – 135Combined sources4
Beta strandi138 – 141Combined sources4
Turni144 – 146Combined sources3
Beta strandi149 – 156Combined sources8
Helixi157 – 159Combined sources3
Beta strandi160 – 162Combined sources3
Helixi169 – 172Combined sources4
Helixi173 – 176Combined sources4
Helixi178 – 187Combined sources10
Turni188 – 190Combined sources3
Beta strandi197 – 201Combined sources5
Helixi205 – 216Combined sources12
Beta strandi220 – 225Combined sources6
Helixi229 – 231Combined sources3
Helixi232 – 235Combined sources4
Helixi236 – 238Combined sources3
Beta strandi242 – 244Combined sources3
Helixi246 – 248Combined sources3
Helixi253 – 260Combined sources8
Beta strandi265 – 270Combined sources6
Helixi275 – 283Combined sources9
Turni287 – 289Combined sources3
Beta strandi291 – 294Combined sources4
Helixi309 – 312Combined sources4
Beta strandi316 – 319Combined sources4
Helixi322 – 324Combined sources3
Helixi327 – 339Combined sources13
Helixi346 – 348Combined sources3
Beta strandi349 – 354Combined sources6
Helixi355 – 358Combined sources4
Helixi359 – 366Combined sources8
Beta strandi371 – 376Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RQTX-ray2.30A6-379[»]
4RQUX-ray2.50A/B6-379[»]
ProteinModelPortaliP06525.
SMRiP06525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
InParanoidiP06525.
KOiK18857.
OMAiGACRIIG.
OrthoDBiEOG09360BVQ.
PhylomeDBiP06525.

Family and domain databases

InterProiView protein in InterPro
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like_sf.
IPR036291. NAD(P)-bd_dom_sf.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00059. ADH_ZINC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06525-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:379
Mass (Da):41,178
Last modified:May 29, 2007 - v2
Checksum:i32550529538B9669
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti154V → L in AAM65556 (Ref. 11) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti43F → Y in strain: cv. Hiroshima. 1 Publication1
Natural varianti51V → L in strain: cv. Bla-10, cv. Ci-0, cv. Cvi-0, cv. Hiroshima, cv. Kas-1 and cv. Ita-0. 3 Publications1
Natural varianti101E → 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 Publications1
Natural varianti106H → K in strain: cv. Bl-1 and cv. Gr-1. 2 Publications1
Natural varianti106H → Q in strain: cv. Aa-0, cv. Al-0, cv. Bs-0, cv. Mt-0, cv. Shokei and cv. Yo-0. 2 Publications1
Natural varianti120T → P in strain: cv. Es-0. 1 Publication1
Natural varianti180S → A in strain: cv. Bla-10. 1 Publication1
Natural varianti197S → T in strain: cv. Cvi-0. 1 Publication1
Natural varianti217A → V in strain: cv. Kas-1. 1 Publication1

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.
PIRiA23815. DEMUAM.
RefSeqiNP_177837.1. NM_106362.3.
UniGeneiAt.22653.
At.64099.

Genome annotation databases

EnsemblPlantsiAT1G77120.1; AT1G77120.1; AT1G77120.
GeneIDi844047.
GrameneiAT1G77120.1; AT1G77120.1; AT1G77120.
KEGGiath:AT1G77120.

Similar proteinsi

Entry informationi

Entry nameiADH1_ARATH
AccessioniPrimary (citable) accession number: P06525
Secondary accession number(s): O04080
, O04713, O04717, O04868, O23821, Q8LA61, Q94AY6, Q9CAZ2, Q9CAZ3, Q9SX08
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 29, 2007
Last modified: November 22, 2017
This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families