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Protein

Alcohol dehydrogenase class-3

Gene
N/A
Organism
Myxine glutinosa (Atlantic hagfish)
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 bindingi47Zinc 1; catalyticBy similarity1
Metal bindingi69Zinc 1; catalyticBy similarity1
Metal bindingi99Zinc 2By similarity1
Metal bindingi102Zinc 2By similarity1
Metal bindingi105Zinc 2By similarity1
Metal bindingi113Zinc 2By similarity1
Sitei117Important for FDH activity and activation by fatty acidsBy similarity1
Metal bindingi176Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
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)
OrganismiMyxine glutinosa (Atlantic hagfish)
Taxonomic identifieri7769 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataCyclostomataHyperotretiMyxiniformesMyxinidaeMyxininaeMyxine

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001607651 – 376Alcohol dehydrogenase class-3Add BLAST376

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylserine2 Publications1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP80360

PTM databases

iPTMnetiP80360

Expressioni

Tissue specificityi

Liver and gut.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP80360
SMRiP80360
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000195

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
IPR020843 PKS_ER
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SMARTiView protein in SMART
SM00829 PKS_ER, 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.

P80360-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
SKMDGQVIHC KAAVAWEAKK PLSLEEIEVA PPKAHEVRMK VLATAVCHTD
60 70 80 90 100
AYTLSGVDPE GSFPVVLGHE GAGIVESVGE GVTKFKPGDS VIPLYIPQCG
110 120 130 140 150
ECKFCLNPKT NLCQKIRVTQ GKGMMPDGTS RLTCRGKSLY HFMGASTFSE
160 170 180 190 200
YAVVADISLC RVAPEAPPDR VCLLGCGVST GYGAPLNTAK VEPGSTCAIF
210 220 230 240 250
GLGAVGLAAI MGCRVAGASR IIAIDRNPDK FEKARIFGAT DCVVPDASDK
260 270 280 290 300
PISQVLGEMT DGGLDYTFEC VGNVGIMRAA LESCHKGWGV SVILGVAGGG
310 320 330 340 350
QEISTRPFQL VTGRTWKGAA FGGWKSVESV PKLVDDYMAG KIMVDEFVSH
360 370
SLPFDSINEA FDLMHAGKSI RTVLQL
Length:376
Mass (Da):39,747
Last modified:February 1, 1995 - v1
Checksum:iFFD20C195FF67B5F
GO

Sequence databases

PIRiS51187

Similar proteinsi

Entry informationi

Entry nameiADHX_MYXGL
AccessioniPrimary (citable) accession number: P80360
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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