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P35630 (ADH1_ENTHI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NADP-dependent isopropanol dehydrogenase
EC=1.1.1.80
Gene names
Name:ADH1
OrganismEntamoeba histolytica
Taxonomic identifier5759 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde. Ref.5

Catalytic activity

Propan-2-ol + NADP+ = acetone + NADPH. Ref.5

Cofactor

Binds 1 zinc ion per subunit. Ref.5

Subunit structure

Homodimer. Ref.3 Ref.5

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NADP
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisopropanol dehydrogenase (NADP+) 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 – 360360NADP-dependent isopropanol dehydrogenase
PRO_0000160695

Regions

Nucleotide binding175 – 1784NADP By similarity
Nucleotide binding198 – 2003NADP By similarity
Nucleotide binding265 – 2673NADP By similarity

Sites

Metal binding371Zinc; catalytic
Metal binding591Zinc; catalytic
Metal binding601Zinc; catalytic
Metal binding1501Zinc; catalytic
Binding site2181NADP By similarity
Binding site3401NADP By similarity

Secondary structure

1 ....................................................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35630 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 6D01643EB4A3A07F

FASTA36038,568
        10         20         30         40         50         60 
MKGLAMLGIG RIGWIEKKIP ECGPLDALVR PLALAPCTSD THTVWAGAIG DRHDMILGHE 

        70         80         90        100        110        120 
AVGQIVKVGS LVKRLKVGDK VIVPAITPDW GEEESQRGYP MHSGGMLGGW KFSNFKDGVF 

       130        140        150        160        170        180 
SEVFHVNEAD ANLALLPRDI KPEDAVMLSD MVTTGFHGAE LANIKLGDTV CVIGIGPVGL 

       190        200        210        220        230        240 
MSVAGANHLG AGRIFAVGSR KHCCDIALEY GATDIINYKN GDIVEQILKA TDGKGVDKVV 

       250        260        270        280        290        300 
IAGGDVHTFA QAVKMIKPGS DIGNVNYLGE GDNIDIPRSE WGVGMGHKHI HGGLTPGGRV 

       310        320        330        340        350        360 
RMEKLASLIS TGKLDTSKLI THRFEGLEKV EDALMLMKNK PADLIKPVVR IHYDDEDTLH

« Hide

References

[1]"Cloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene of Entamoeba histolytica."
Kumar A., Shen P.S., Descoteaux S., Pohl J., Bailey G., Samuelson J.
Proc. Natl. Acad. Sci. U.S.A. 89:10188-10192(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Primary structures of alcohol and aldehyde dehydrogenase genes of Entamoeba histolytica."
Samuelson J., Zhang W.W., Kumar A., Descoteaux S., Shen P.S., Bailey G.
Arch. Med. Res. 23:31-33(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of alcohol dehydrogenase from Entamoeba histolytica."
Shimon L.J.W., Goihberg E., Peretz M., Burstein Y., Frolow F.
Acta Crystallogr. D 62:541-547(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT.
[4]"Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution."
Goihberg E., Dym O., Tel-Or S., Shimon L., Frolow F., Peretz M., Burstein Y.
Proteins 72:711-719(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
[5]"Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms."
Goihberg E., Peretz M., Tel-Or S., Dym O., Shimon L., Frolow F., Burstein Y.
Biochemistry 49:1943-1953(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M88600 mRNA. Translation: AAA51479.1.
PIRA46409.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y9AX-ray1.81A/C1-360[»]
2OUIX-ray1.77A/B/C/D1-360[»]
3FPCX-ray1.40A/B/C/D153-294[»]
ProteinModelPortalP35630.
SMRP35630. Positions 1-360.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1063.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
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]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35630.

Entry information

Entry nameADH1_ENTHI
AccessionPrimary (citable) accession number: P35630
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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