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Protein

Alcohol dehydrogenase class-3

Gene

Adh5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.

Catalytic activityi

A primary alcohol + NAD+ = an aldehyde + NADH.
A secondary alcohol + NAD+ = a ketone + NADH.
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Zinc 1; catalyticBy similarity1
Metal bindingi67Zinc 1; catalyticBy similarity1
Metal bindingi97Zinc 2By similarity1
Metal bindingi100Zinc 2By similarity1
Metal bindingi103Zinc 2By similarity1
Metal bindingi111Zinc 2By similarity1
Sitei115Important for FDH activity and activation by fatty acidsBy similarity1
Metal bindingi174Zinc 1; catalyticBy similarity1

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: MGI
  • fatty acid binding Source: MGI
  • formaldehyde dehydrogenase activity Source: MGI
  • protein homodimerization activity Source: MGI
  • S-(hydroxymethyl)glutathione dehydrogenase activity Source: MGI
  • zinc ion binding Source: MGI

GO - Biological processi

  • ethanol catabolic process Source: MGI
  • ethanol oxidation Source: InterPro
  • formaldehyde catabolic process Source: MGI
  • peptidyl-cysteine S-nitrosylation Source: MGI
  • positive regulation of blood pressure Source: MGI
  • respiratory system process Source: MGI
  • response to lipopolysaccharide Source: MGI
  • response to nitrosative stress Source: MGI
  • response to redox state Source: MGI
  • retinoid metabolic process Source: MGI

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-71384 Ethanol oxidation

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase 2
Alcohol dehydrogenase 5
Alcohol dehydrogenase B2
Short name:
ADH-B2
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase (EC:1.1.1.-)
Short name:
FALDH
Short name:
FDH
Short name:
GSH-FDH
S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284)
Gene namesi
Name:Adh5
Synonyms:Adh-2, Adh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:87929 Adh5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001607602 – 374Alcohol dehydrogenase class-3Add BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei233N6-succinyllysineCombined sources1
Modified residuei247PhosphoserineCombined sources1
Modified residuei315N6-succinyllysineCombined sources1
Modified residuei324PhosphoserineBy similarity1
Modified residuei351PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP28474
PaxDbiP28474
PeptideAtlasiP28474
PRIDEiP28474

2D gel databases

REPRODUCTION-2DPAGEiP28474

PTM databases

iPTMnetiP28474
PhosphoSitePlusiP28474
SwissPalmiP28474

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSMUSG00000028138
ExpressionAtlasiP28474 baseline and differential
GenevisibleiP28474 MM

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

IntActiP28474, 2 interactors
MINTiP28474
STRINGi10090.ENSMUSP00000005964

Structurei

3D structure databases

ProteinModelPortaliP28474
SMRiP28474
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022 Eukaryota
COG1062 LUCA
GeneTreeiENSGT00430000030800
HOGENOMiHOG000294674
HOVERGENiHBG000195
InParanoidiP28474
KOiK00121
OMAiCIGNVNT
OrthoDBiEOG091G08N3
PhylomeDBiP28474
TreeFamiTF300429

Family and domain databases

CDDicd08300 alcohol_DH_class_III, 1 hit
InterProiView protein in InterPro
IPR014183 ADH_3
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SUPFAMiSSF50129 SSF50129, 2 hits
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR02818 adh_III_F_hyde, 1 hit
PROSITEiView protein in PROSITE
PS00059 ADH_ZINC, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY
60 70 80 90 100
TLSGADPEGC FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC
110 120 130 140 150
KFCLNPKTNL CQKIRVTQGK GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT
160 170 180 190 200
VVADISVAKI DPSAPLDKVC LLGCGISTGY GAAVNTAKVE PGSTCAVFGL
210 220 230 240 250
GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC ISPQDFSKSI
260 270 280 290 300
QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE
310 320 330 340 350
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL
360 370
SFDQINQAFD LMHSGDSIRT VLKM
Length:374
Mass (Da):39,548
Last modified:January 23, 2007 - v3
Checksum:i32A3727B5DAB0919
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55A → R no nucleotide entry (PubMed:2053480).Curated1
Sequence conflicti55A → R in AAA68896 (PubMed:1472709).Curated1
Sequence conflicti55A → R in AAC52763 (PubMed:8647091).Curated1
Sequence conflicti133K → R in BAE35383 (PubMed:16141072).Curated1
Sequence conflicti183A → T in BAE35383 (PubMed:16141072).Curated1
Sequence conflicti253V → I in BAE35383 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84147 mRNA Translation: AAA68896.1
U48970
, U48964, U48965, U48966, U48968, U48969 Genomic DNA Translation: AAC52763.1
AK076507 mRNA Translation: BAC36370.1
AK146949 mRNA Translation: BAE27558.1
AK159803 mRNA Translation: BAE35383.1
BC090978 mRNA Translation: AAH90978.1
CCDSiCCDS17868.1
PIRiA56643
RefSeqiNP_001275507.1, NM_001288578.1
NP_031436.2, NM_007410.3
UniGeneiMm.3874

Genome annotation databases

EnsembliENSMUST00000005964; ENSMUSP00000005964; ENSMUSG00000028138
GeneIDi11532
KEGGimmu:11532
UCSCiuc008rnk.2 mouse

Similar proteinsi

Entry informationi

Entry nameiADHX_MOUSE
AccessioniPrimary (citable) accession number: P28474
Secondary accession number(s): Q3TW83, Q8C662
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 168 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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