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P22797 (ADH1_PELPE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 73. 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
Alternative name(s):
Alcohol dehydrogenase, major
OrganismPelophylax perezi (Perez's frog) (Rana perezi)
Taxonomic identifier8403 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Raninae › Rana › Pelophylax

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

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
   PTMAcetylation
   Technical termDirect protein sequencing
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

Chain1 – 375375Alcohol dehydrogenase 1
PRO_0000160680

Regions

Nucleotide binding200 – 2056NAD By similarity
Nucleotide binding293 – 2953NAD By similarity

Sites

Metal binding461Zinc 1; catalytic By similarity
Metal binding681Zinc 1; catalytic By similarity
Metal binding981Zinc 2 By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1121Zinc 2 By similarity
Metal binding1751Zinc 1; catalytic By similarity
Binding site2241NAD By similarity
Binding site2291NAD By similarity
Binding site3701NAD By similarity

Amino acid modifications

Modified residue11N-acetylalanine Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22797 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 283E0A60E3339195

FASTA37540,185
        10         20         30         40         50         60 
ATAGKVIKCK AAVCWGPKQP LSIEEIEVAP PKRHEVRVKI VATGICRSDD HVISGALSDM 

        70         80         90        100        110        120 
KFPVILGHEA AGVVESVGEG VTKFKPGDKV IPLFVPQCGE CRCCKNPESN LCYKNDIGKY 

       130        140        150        160        170        180 
DGVLLDKTSR FTCKGKSIHN FISTSTFTEY TVLDEIAVAK IHEDAPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVNTGKV KPGSTCAVFG LGGVGLSVII GCKVAGASRI IGVDLNSDKF TTAKECGATE 

       250        260        270        280        290        300 
CINPKDYNIP IHEVLAKMTD DGVDYAFEVI GNTTVMTSAL SSSHFGCGKT VIVGLAPSSA 

       310        320        330        340        350        360 
VMSFDPLLIL TGRILTGAVF GGWKSKDDVP KLVRDYLNKK FDFDPLITHY MPFEKINEGF 

       370 
ELLRNGKSIR TILTF

« Hide

References

[1]"Amphibian alcohol dehydrogenase, the major frog liver enzyme. Relationships to other forms and assessment of an early gene duplication separating vertebrate class I and class III alcohol dehydrogenases."
Cederlund E., Peralba J.M., Pares X., Joernvall H.
Biochemistry 30:2811-2816(1991) [PubMed: 2007119] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Fast atom bombardment mass spectrometry and chemical analysis in determinations of acyl-blocked protein structures."
Egestad B., Estonius M., Danielsson O., Persson B., Cederlund E., Kaiser R., Holmquist B., Vallee B., Pares X., Jefferey J., Joernvall H.
FEBS Lett. 269:194-196(1990) [PubMed: 2387402] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-5.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA38405.
S11075.

3D structure databases

ProteinModelPortalP22797.
SMRP22797. Positions 1-375.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000195.

Family and domain databases

InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
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.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH1_PELPE
AccessionPrimary (citable) accession number: P22797
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: December 14, 2011
This is version 73 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

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