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Reviewed, UniProtKB/Swiss-Prot P26325 (ADH1_GADCA)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismGadus callarias (Baltic cod)
Taxonomic identifier8053 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Paracanthopterygii › Gadiformes › Gadidae › Gadus

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Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Miscellaneous

Functionally related to class-I mammalian enzymes, but structurally related to class-III.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
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 – 375375Alcohol dehydrogenase 1
PRO_0000160679

Regions

Nucleotide binding200 – 2056NAD
Nucleotide binding293 – 2953NAD

Sites

Metal binding461Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1751Zinc 1; catalytic
Binding site2241NAD
Binding site2291NAD
Binding site3691NAD

Amino acid modifications

Modified residue11N-acetylalanine Ref.1

Secondary structure

1 ............................................................................... 375
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P26325-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 0A8BDEAA0C9BCEAD

FASTA37540,128
        10         20         30         40         50         60 
ATVGKVIKCK AAVAWEANKP LVIEEIEVDV PHANEIRIKI IATGVCHTDL YHLFEGKHKD 

        70         80         90        100        110        120 
GFPVVLGHEG AGIVESVGPG VTEFQPGEKV IPLFISQCGE CRFCQSPKTN QCVKGWANES 

       130        140        150        160        170        180 
PDVMSPKETR FTCKGRKVLQ FLGTSTFSQY TVVNQIAVAK IDPSAPLDTV CLLGCGVSTG 

       190        200        210        220        230        240 
FGAAVNTAKV EPGSTCAVFG LGAVGLAAVM GCHSAGAKRI IAVDLNPDKF EKAKVFGATD 

       250        260        270        280        290        300 
FVNPNDHSEP ISQVLSKMTN GGVDFSLECV GNVGVMRNAL ESCLKGWGVS VLVGWTDLHD 

       310        320        330        340        350        360 
VATRPIQLIA GRTWKGSMFG GFKGKDGVPK MVKAYLDKKV KLDEFITHRM PLESVNDAID 

       370 
LMKHGKCIRT VLSLE

« Hide

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References

[1]"The major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammalian alcohol dehydrogenases of classes I and III."
Danielsson O., Eklund H., Joernvall H.
Biochemistry 31:3751-3759(1992) [PubMed: 1567829] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Crystal structure of cod liver class I alcohol dehydrogenase: substrate pocket and structurally variable segments."
Ramaswamy S., el Ahmad M., Danielsson O., Joernvall H., Eklund H.
Protein Sci. 5:663-671(1996) [PubMed: 8845755] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
Tissue: Liver.

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Cross-references

Sequence databases

PIRA42343.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CDOX-ray2.05A/B1-374[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP26325.

Enzyme and pathway databases

BRENDA1.1.1.1. 39196.

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_GADCA
AccessionPrimary (citable) accession number: P26325
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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