Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P35630 (ADH1_ENTHI)

Last modified June 16, 2009. Version 55. 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

Names and origin

Protein namesRecommended name:
    NADP-dependent alcohol dehydrogenase
    EC=1.1.1.2
Gene names
Name: ADH1
OrganismEntamoeba histolytica
Taxonomic identifier5759 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaArchamoebaeEntamoebidaeEntamoeba

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

An alcohol + NADP+ = an aldehyde + NADPH.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer. Ref.3

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)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360NADP-dependent alcohol dehydrogenase
PRO_0000160695

Regions

Nucleotide binding174 – 1796NAD By similarity
Nucleotide binding265 – 2673NAD By similarity

Sites

Metal binding371Zinc; catalytic
Metal binding591Zinc; catalytic
Metal binding601Zinc; catalytic
Metal binding1501Zinc; catalytic

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P35630-1 [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: 1438208] [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: 1340318] [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: 16627948] [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."
Protein structure factory (PSF)
Submitted (FEB-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

M88600 mRNA. Translation: AAA51479.1.
PIRA46409.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1Y9AX-ray1.81A/C1-360[»]
2OUIX-ray1.77A/B/C/D1-360[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.2. 323.

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...

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: June 16, 2009
This is version 55 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents