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P30350 (ADH1_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 1

EC=1.1.1.1
Gene names
Name:ADH1
OrganismAnas platyrhynchos (Domestic duck) (Anas boschas)
Taxonomic identifier8839 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas

Protein attributes

Sequence length185 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 185›185Alcohol dehydrogenase 1
PRO_0000160670

Regions

Nucleotide binding10 – 156NAD By similarity
Nucleotide binding103 – 1053NAD By similarity

Sites

Binding site341NAD By similarity
Binding site391NAD By similarity
Binding site1801NAD By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P30350 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: BDA5DF3534C6192D

FASTA18519,816
        10         20         30         40         50         60 
ARGSTCAVFG LGGVGLSVIM GCKAAGASRI IAVDINSDKF AKAKELGATD CINPKDHKEP 

        70         80         90        100        110        120 
IHKVLIGMTG YGVDYSFEVI GRIETMVAAL ASCHYNYGVS VIVGVPPAAQ NITFDPMLLF 

       130        140        150        160        170        180 
SGRTWKGSVF GGWKSKDSVP KLVADYMKKK FVLDPLITHT LPFSKINEGF DLLRAGKSIR 


SVLTF 

« Hide

References

[1]"Estrogen induction of alcohol dehydrogenase in the uropygial gland of mallard ducks."
Hiremath L.S., Kessler P.M., Sasaki G.C., Kolattukudy P.E.
Eur. J. Biochem. 203:449-457(1992) [PubMed: 1370936] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Uropygial gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63948 mRNA. Translation: CAA45373.1.
PIRS20593.

3D structure databases

ProteinModelPortalP30350.
SMRP30350. Positions 2-185.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000195.

Family and domain databases

InterProIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH1_ANAPL
AccessionPrimary (citable) accession number: P30350
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 14, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families