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P00327 (ADH1E_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
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

Initiator methionine11Removed Ref.2
Chain2 – 375374Alcohol dehydrogenase E chain
PRO_0000160656

Regions

Nucleotide binding200 – 2056NAD
Nucleotide binding293 – 2953NAD

Sites

Metal binding471Zinc 1; catalytic Ref.3
Metal binding681Zinc 1; catalytic Ref.3
Metal binding981Zinc 2 Ref.3
Metal binding1011Zinc 2 Ref.3
Metal binding1041Zinc 2 Ref.3
Metal binding1121Zinc 2 Ref.3
Metal binding1751Zinc 1; catalytic
Binding site2241NAD
Binding site2291NAD
Binding site3701NAD

Amino acid modifications

Modified residue21N-acetylserine Ref.2

Secondary structure

1 ......................................................................................... 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00327 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DA701D2F6AB69C9D

FASTA37539,936
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEEKK PFSIEEVEVA PPKAHEVRIK MVATGICRSD DHVVSGTLVT 

        70         80         90        100        110        120 
PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFTPQCGK CRVCKHPEGN FCLKNDLSMP 

       130        140        150        160        170        180 
RGTMQDGTSR FTCRGKPIHH FLGTSTFSQY TVVDEISVAK IDAASPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVKVAKV TQGSTCAVFG LGGVGLSVIM GCKAAGAARI IGVDINKDKF AKAKEVGATE 

       250        260        270        280        290        300 
CVNPQDYKKP IQEVLTEMSN GGVDFSFEVI GRLDTMVTAL SCCQEAYGVS VIVGVPPDSQ 

       310        320        330        340        350        360 
NLSMNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FALDPLITHV LPFEKINEGF 

       370 
DLLRSGESIR TILTF

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-375.
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[5]"Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8-A resolution."
Al-Karadaghi S., Cedergren-Zeppezauer E.S., Hovmoeller S., Petratos K., Terry H., Wilson K.S.
Acta Crystallogr. D 50:793-807(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M64864 mRNA. Translation: AAA30931.1.
PIRDEHOAL. A39872.
RefSeqNP_001075997.1. NM_001082528.1.
UniGeneEca.13382.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A71X-ray2.00A/B2-374[»]
1A72X-ray2.60A2-374[»]
1ADBX-ray2.40A/B2-374[»]
1ADCX-ray2.70A/B2-374[»]
1ADFX-ray2.90A2-374[»]
1ADGX-ray2.70A2-374[»]
1AXEX-ray2.00A/B2-374[»]
1AXGX-ray2.50A/B/C/D2-374[»]
1BTOX-ray2.00A/B/C/D2-374[»]
1HETX-ray1.15A/B2-375[»]
1HEUX-ray1.15A/B2-375[»]
1HF3X-ray1.95A/B2-375[»]
1HLDX-ray2.10A/B2-374[»]
1JU9X-ray2.00A/B2-374[»]
1LDEX-ray2.50A/B/C/D2-374[»]
1LDYX-ray2.50A/B/C/D2-374[»]
1MG0X-ray1.80A/B/C/D2-374[»]
1MGOX-ray1.20A/B2-374[»]
1N8KX-ray1.13A/B2-374[»]
1N92X-ray1.47A/B2-374[»]
1P1RX-ray1.57A/B/C/D2-374[»]
1QLHX-ray2.07A2-375[»]
1QLJX-ray2.80A2-375[»]
1QV6X-ray1.80A/B2-374[»]
1QV7X-ray1.80A/B2-374[»]
1YE3X-ray1.59A2-374[»]
2JHFX-ray1.00A/B2-374[»]
2JHGX-ray1.20A/B2-374[»]
2OHXX-ray1.80A/B2-375[»]
2OXIX-ray2.10A/B2-374[»]
3BTOX-ray1.66A/B/C/D2-374[»]
3OQ6X-ray1.20A/B2-375[»]
4DWVX-ray1.14A/B2-375[»]
4DXHX-ray1.12A/B2-375[»]
5ADHX-ray2.90A2-374[»]
6ADHX-ray2.90A/B2-374[»]
7ADHX-ray3.20A2-374[»]
8ADHX-ray2.40A2-374[»]
ProteinModelPortalP00327.
SMRP00327. Positions 2-375.
ModBaseSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000017080.

Proteomic databases

PRIDEP00327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100034242.
KEGGecb:100034242.

Phylogenomic databases

eggNOGCOG1062.
HOGENOMHOG000294674.
HOVERGENHBG000195.
InParanoidP00327.
KOK13951.
OrthoDBEOG4BRWM5.

Enzyme and pathway databases

SABIO-RKP00327.

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. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP00327.
ChEMBLCHEMBL2624.
DrugBankDB01093. Dimethyl sulfoxide.
EvolutionaryTraceP00327.

Entry information

Entry nameADH1E_HORSE
AccessionPrimary (citable) accession number: P00327
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents