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Reviewed, UniProtKB/Swiss-Prot O57380 (ADH8_RANPE)

Last modified June 16, 2009. Version 62. 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:
    NADP-dependent alcohol dehydrogenase
    EC=1.1.1.2
Gene names
Name: ADH8
OrganismRana perezi (Perez's frog) (Western Mediterranian green frog)
Taxonomic identifier8403 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Rana › Pelophylax

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Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

An alcohol + NADP+ = an aldehyde + NADPH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer.

Sequence similarities

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

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Ontologies

Keywords
   LigandMetal-binding
NADP
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalcohol dehydrogenase (NADP+) 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

Initiator methionine11Removed Ref.1
Chain2 – 373372NADP-dependent alcohol dehydrogenase
PRO_0000160756

Sites

Metal binding471Zinc 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 binding1741Zinc 1; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylcysteine By similarity

Experimental info

Sequence conflict741V → L AA sequence Ref.1
Sequence conflict1341R → K AA sequence Ref.1
Sequence conflict1421V → M AA sequence Ref.1

Secondary structure

1 ............................................................................. 373
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O57380-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 954A502267E8DE49

FASTA37339,168
        10         20         30         40         50         60 
MCTAGKDITC KAAVAWEPHK PLSLETITVA PPKAHEVRIK ILASGICGSD SSVLKEIIPS 

        70         80         90        100        110        120 
KFPVILGHEA VGVVESIGAG VTCVKPGDKV IPLFVPQCGS CRACKSSNSN FCEKNDMGAK 

       130        140        150        160        170        180 
TGLMADMTSR FTCRGKPIYN LVGTSTFTEY TVVADIAVAK IDPKAPLESC LIGCGFATGY 

       190        200        210        220        230        240 
GAAVNTAKVT PGSTCAVFGL GGVGFSAIVG CKAAGASRII GVGTHKDKFP KAIELGATEC 

       250        260        270        280        290        300 
LNPKDYDKPI YEVICEKTNG GVDYAVECAG RIETMMNALQ STYCGSGVTV VLGLASPNER 

       310        320        330        340        350        360 
LPLDPLLLLT GRSLKGSVFG GFKGEEVSRL VDDYMKKKIN VNFLVSTKLT LDQINKAFEL 

       370 
LSSGQGVRSI MIY

« Hide

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References

[1]"Structural and enzymatic properties of a gastric NADP(H)-dependent and retinal-active alcohol dehydrogenase."
Peralba J.M., Cederlund E., Crosas B., Moreno A., Julia P., Martinez S.E., Persson B., Farres J., Pares X., Joernvall H.
J. Biol. Chem. 274:26021-26026(1999) [PubMed: 10473548] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-373.
Tissue: Stomach.
[2]"Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi."
Valencia E., Rosell A., Larroy C., Farres J., Biosca J.A., Fita I., Pares X., Ochoa W.F.
Acta Crystallogr. D 59:334-337(2003) [PubMed: 12554944] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

AJ002554 mRNA. Translation: CAA05553.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1P0CX-ray2.20A/B1-373[»]
1P0FX-ray1.80A/B1-373[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENO57380.

Enzyme and pathway databases

BRENDA1.1.1.2. 189765.

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 nameADH8_RANPE
AccessionPrimary (citable) accession number: O57380
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 62 of the entry and version 3 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