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LOC100034242 alcohol dehydrogenase-E-isoenzyme [ Equus caballus (horse) ]

Gene ID: 100034242, updated on 11-Apr-2024

Summary

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Gene symbol
LOC100034242
Gene description
alcohol dehydrogenase-E-isoenzyme
See related
Ensembl:ENSECAG00000034047
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Equus caballus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus
Also known as
ADH1E
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Genomic context

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See LOC100034242 in Genome Data Viewer
Location:
chromosome: 3
Exon count:
9
Annotation release Status Assembly Chr Location
103 current EquCab3.0 (GCF_002863925.1) 3 NC_009146.3 (40667230..40682661)
102 previous assembly EquCab2.0 (GCF_000002305.2) 3 NC_009146.2 (40054604..40070120)

Chromosome 3 - NC_009146.3Genomic Context describing neighboring genes Neighboring gene chromosome 3 C4orf17 homolog Neighboring gene alcohol dehydrogenase class 4 mu/sigma chain-like Neighboring gene uncharacterized LOC111772840 Neighboring gene alcohol dehydrogenase-S-isoenzyme

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis. Plapp BV, et al. Biochemistry, 2017 Jul 18. PMID 28640600, Free PMC Article
  2. Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93. Kim K, et al. Chem Biol Interact, 2017 Oct 1. PMID 28025168, Free PMC Article
  3. Atomic-resolution structures of horse liver alcohol dehydrogenase with NAD(+) and fluoroalcohols define strained Michaelis complexes. Plapp BV, et al. Biochemistry, 2012 May 15. PMID 22531044, Free PMC Article
  4. Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolution. Al-Karadaghi S, et al. Acta Crystallogr D Biol Crystallogr, 1994 Nov 1. PMID 15299346
  5. Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Eklund H, et al. Biochemistry, 1984 Dec 4. PMID 6098306

See all (8) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The S48T/F93A substitutions of ADH1E (alcohol dehydrogenase 1E) invert the enantioselectivity for alcohol oxidation, increasing the R/S ratio by 10, 590, and 200-fold for 2-butanol, 2-octanol, and sec-phenethyl alcohol.
    Title: Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93.
  2. In liver alcohol dehydrogenase with NAD(+) the nicotinamide ring is strained toward the transition state on the path to alcohol oxidation.
    Title: Atomic-resolution structures of horse liver alcohol dehydrogenase with NAD(+) and fluoroalcohols define strained Michaelis complexes.
  3. The enzyme-NADH complex has a closed conformation similar to that of ternary complexes with coenzyme and substrate analogues; the coordination of the catalytic zinc is similar to that found in the apoenzyme, except that a minor, alternative position for the catalytic zinc is approximately 1.3 A from the major position and closer to Glu-68, which could form the alternative coordination to the catalytic zinc.
    Title: Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.
Submit: New GeneRIF Correction

General gene information

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Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables alcohol dehydrogenase (NAD+) activity, zinc-dependent IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables all-trans-retinol dehydrogenase (NAD+) activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in retinoic acid metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in retinol metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
alcohol dehydrogenase E chain
Names
Alcohol dehydrogenase S chain
alcohol dehydrogenase-S-isoenzyme
NP_001075997.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001082528.1 → NP_001075997.1  alcohol dehydrogenase E chain

    See identical proteins and their annotated locations for NP_001075997.1

    Status: PROVISIONAL

    Source sequence(s)
    M64864
    UniProtKB/Swiss-Prot
    P00327
    UniProtKB/TrEMBL
    A0A9L0SIF1
    Related
    ENSECAP00000036157.2, ENSECAT00000057279.3
    Conserved Domains (1) summary
    cd08299
    Location:3 → 375
    alcohol_DH_class_I_II_IV; class I, II, IV alcohol dehydrogenases

RefSeqs of Annotated Genomes: Equus caballus Annotation Release 103 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference EquCab3.0 Primary Assembly

Genomic

  1. NC_009146.3 Reference EquCab3.0 Primary Assembly

    Range
    40667230..40682661
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00327.2 GenPept UniProtKB/Swiss-Prot:P00327
P00328.3 GenPept UniProtKB/Swiss-Prot:P00328

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases