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Reviewed, UniProtKB/Swiss-Prot P25141 (ADH1_PETHY)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Gene names
Name: ADH1
OrganismPetunia hybrida (Petunia)
Taxonomic identifier4102 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Petunioideae › Petunia

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Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

This protein is responsible for the conversion of alcohols to aldehydes in plants and is important for NAD metabolism during anaerobic respiration.

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Alcohol dehydrogenase 1
PRO_0000160711

Regions

Nucleotide binding204 – 2096NAD By similarity
Nucleotide binding298 – 3003NAD By similarity

Sites

Metal binding491Zinc 1; catalytic By similarity
Metal binding711Zinc 1; catalytic By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1151Zinc 2 By similarity
Metal binding1791Zinc 1; catalytic By similarity
Binding site2281NAD By similarity
Binding site2331NAD By similarity
Binding site3751NAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
P25141-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 43DFFE215650EDE0

FASTA38241,574
        10         20         30         40         50         60 
MSSNTAGQVI RCKAAVAWEA GKPLVIEEVE VAPPQKMEVR LKILFTSLCH TDVYFWEAKG 

        70         80         90        100        110        120 
QTPLFPRIFG HEAGGIVESV GEGVTDLKPG DHVLPVFTGE CQQCRHCKSE ESNMCDLLRI 

       130        140        150        160        170        180 
NTDRGVMIHD GQTRFSKDGK PIYHFVGTST FSEYTVCHSG CVTKIDPQAP LDKVCVLSCG 

       190        200        210        220        230        240 
ISTGLGATLN VAKPTKGSTV AIFGLGAVGL AAAEGARIAG ASRIIGVDLN PSRFNDAKKF 

       250        260        270        280        290        300 
GVTEFVNPKD HGDKPVQQVI AEMTDGGVDR SVECTGNVNA MISAFECVHD GWGVAVLVGV 

       310        320        330        340        350        360 
PNKDDAFKTH PMNLLNERTL KGTFFGNYKP KSDIPSVVDK YMKKELELEK FITHQVPFSE 

       370        380 
INKAFDYMLK GESIRCMITM EH

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References

[1]"Structure, expression, chromosomal location and product of the gene encoding ADH1 in Petunia."
Gregerson R., McLean M., Beld M., Gerats A.G.M., Strommer J.
Plant Mol. Biol. 17:37-48(1991) [PubMed: 1678286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Violet 30.

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Cross-references

Sequence databases

X54106 Genomic DNA. Translation: CAA38039.1.
PIRDEPJA1. S16596.

3D structure databases

HSSPHSSP built from PDB template 1M6H based on UniProtKB P11766.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.1. 2263.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADH1_PETHY
AccessionPrimary (citable) accession number: P25141
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents