Skip Header

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

Reviewed, UniProtKB/Swiss-Prot P00328 (ADH1S_HORSE)

Last modified June 16, 2009. Version 84. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase S chain
    EC=1.1.1.1
OrganismEquus caballus (Horse)
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Hide | Top

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.

Subcellular location

Cytoplasm.

Sequence similarities

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

Hide | Top

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

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 374373Alcohol dehydrogenase S chain
PRO_0000160657

Regions

Nucleotide binding199 – 2046NAD
Nucleotide binding292 – 2943NAD

Sites

Metal binding471Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1741Zinc 1; catalytic
Binding site2231NAD
Binding site2281NAD
Binding site3691NAD

Amino acid modifications

Modified residue21N-acetylserine Ref.2

Experimental info

Sequence conflict441A → T AA sequence Ref.2
Sequence conflict601A → T AA sequence Ref.2
Sequence conflict1161L → SL AA sequence Ref.2
Sequence conflict1721V → I AA sequence Ref.2
Sequence conflict2771A → T AA sequence Ref.2

Secondary structure

1 ............................................................................ 374
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P00328-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2B15710A038DA013

FASTA37439,623
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEQKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD DHVVSGTLVA 

        70         80         90        100        110        120 
PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFIPQCGK CSVCKHPEGN LCLKNLSMPR 

       130        140        150        160        170        180 
GTMQDGTSRF TCRGKPIHHF LGTSTFSQYT VVDEISVAKI DAASPLEKVC LVGCGFSTGY 

       190        200        210        220        230        240 
GSAVKVAKVT QGSTCAVFGL GGVGLSVIMG CKAAGAARII GVDINKDKFA KAKEVGATEC 

       250        260        270        280        290        300 
VNPQDYKKPI QEVLTEMSNG GVDFSFEVIG RLDTMVAALS CCQEAYGVSV IVGVPPDSQN 

       310        320        330        340        350        360 
LSMNPMLLLS GRTWKGAIFG GFKSKDSVPK LVADFMAKKF ALDPLITHVL PFEKINEGFD 

       370 
LLRSGKSIRT ILTF

« Hide

Hide | Top

References

[1]"Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites."
Park D.H., Plapp B.V.
J. Biol. Chem. 266:13296-13302(1991) [PubMed: 1712777] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes."
Joernvall H.
Eur. J. Biochem. 16:41-49(1970) [PubMed: 5466062] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-374.
Tissue: Liver.
[3]"Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4-A resolution."
Eklund H., Nordstroem B., Zeppezauer E., Soederlund G., Ohlsson I., Boiwe T., Soederberg B.-O., Tapia O., Braenden C.-I., Aakeson A.
J. Mol. Biol. 102:27-59(1976) [PubMed: 178875] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]"Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase."
Eklund H., Samama J.-P., Jones T.A.
Biochemistry 23:5982-5996(1984) [PubMed: 6098306] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

M64865 mRNA. Translation: AAA30932.1.
PIRDEHOAS. B39872.
RefSeqNP_001075414.1.
UniGeneEca.13101

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EE2X-ray1.54A/B2-373[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSECAG00000019267. Equus caballus. [Contig view]
GeneID100034175.
KEGGecb:100034175.

Phylogenomic databases

HOVERGENP00328.

Enzyme and pathway databases

BRENDA1.1.1.1. 1464.

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...

Hide | Top

Entry information

Entry nameADH1S_HORSE
AccessionPrimary (citable) accession number: P00328
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

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