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Protein

Alcohol dehydrogenase class-3

Gene

Fdh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

An alcohol + NAD+ = an aldehyde or ketone + NADH.
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.
1-octanol + NAD+ = 1-octanal + NADH.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Zinc 1; catalyticBy similarity
Metal bindingi70 – 701Zinc 1; catalyticBy similarity
Metal bindingi100 – 1001Zinc 2By similarity
Metal bindingi103 – 1031Zinc 2By similarity
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi114 – 1141Zinc 2By similarity
Metal bindingi177 – 1771Zinc 1; catalyticBy similarity

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: FlyBase
  • octanol dehydrogenase activity Source: FlyBase
  • S-(hydroxymethyl)glutathione dehydrogenase activity Source: FlyBase
  • S-nitrosoglutathione reductase activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • alcohol metabolic process Source: FlyBase
  • ethanol oxidation Source: InterPro
  • regulation of nitric oxide metabolic process Source: FlyBase
  • regulation of peptidyl-cysteine S-nitrosylation Source: FlyBase
  • visual learning Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-DME-2161541. Abacavir metabolism.
R-DME-5365859. RA biosynthesis pathway.
R-DME-71384. Ethanol oxidation.
SABIO-RKP46415.

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
Octanol dehydrogenase (EC:1.1.1.73)
S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284)
Gene namesi
Name:Fdh
Synonyms:gfd, ODH
ORF Names:CG6598
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0011768. Fdh.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 379378Alcohol dehydrogenase class-3PRO_0000160769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCurated

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP46415.
PRIDEiP46415.

Expressioni

Gene expression databases

BgeeiP46415.
GenevisibleiP46415. DM.

Interactioni

Protein-protein interaction databases

BioGridi66455. 3 interactions.
DIPiDIP-23839N.
IntActiP46415. 1 interaction.
MINTiMINT-1685399.
STRINGi7227.FBpp0081767.

Structurei

3D structure databases

ProteinModelPortaliP46415.
SMRiP46415. Positions 7-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
GeneTreeiENSGT00430000030800.
InParanoidiP46415.
KOiK00121.
OMAiMITHVLK.
OrthoDBiEOG72NRQ6.
PhylomeDBiP46415.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46415-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATEGKVIT CKAAVAWEAK KPLVIEDIEV APPKAHEVRI KITATGVCHT
60 70 80 90 100
DAFTLSGADP EGLFPVVLGH EGAGIVESVG EGVTNFKAGD HVIALYIPQC
110 120 130 140 150
NECKFCKSGK TNLCQKIRLT QGAGVMPEGT SRLSCKGQQL FHFMGTSTFA
160 170 180 190 200
EYTVVADISL TKINEKAPLE KVCLLGCGIS TGYGAALNTA KVEAGSTCAV
210 220 230 240 250
WGLGAVGLAV GLGCKKAGAG KIYGIDINPD KFELAKKFGF TDFVNPKDVA
260 270 280 290 300
DKGSIQNYLI DLTDGGFDYT FECIGNVNTM RSALEATHKG WGTSVVIGVA
310 320 330 340 350
GAGQEISTRP FQLVVGRVWK GSAFGGWRSV SDVPKLVEDY LKKDLLVDEF
360 370
ITHELPLSQI NEAFDLMHKG ESIRSIIKY
Length:379
Mass (Da):40,389
Last modified:January 23, 2007 - v3
Checksum:i7F382E10BFACAAC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07799 Genomic DNA. Translation: AAA57187.1.
U07641 mRNA. Translation: AAB02520.1.
AE014297 Genomic DNA. Translation: AAF54571.1.
AY089518 mRNA. Translation: AAL90256.1.
AY089615 mRNA. Translation: AAL90353.1.
PIRiS51357.
RefSeqiNP_524310.1. NM_079586.4.
UniGeneiDm.1782.

Genome annotation databases

EnsemblMetazoaiFBtr0082290; FBpp0081767; FBgn0011768.
GeneIDi41311.
KEGGidme:Dmel_CG6598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07799 Genomic DNA. Translation: AAA57187.1.
U07641 mRNA. Translation: AAB02520.1.
AE014297 Genomic DNA. Translation: AAF54571.1.
AY089518 mRNA. Translation: AAL90256.1.
AY089615 mRNA. Translation: AAL90353.1.
PIRiS51357.
RefSeqiNP_524310.1. NM_079586.4.
UniGeneiDm.1782.

3D structure databases

ProteinModelPortaliP46415.
SMRiP46415. Positions 7-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66455. 3 interactions.
DIPiDIP-23839N.
IntActiP46415. 1 interaction.
MINTiMINT-1685399.
STRINGi7227.FBpp0081767.

Proteomic databases

PaxDbiP46415.
PRIDEiP46415.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082290; FBpp0081767; FBgn0011768.
GeneIDi41311.
KEGGidme:Dmel_CG6598.

Organism-specific databases

CTDi41311.
FlyBaseiFBgn0011768. Fdh.

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
GeneTreeiENSGT00430000030800.
InParanoidiP46415.
KOiK00121.
OMAiMITHVLK.
OrthoDBiEOG72NRQ6.
PhylomeDBiP46415.

Enzyme and pathway databases

ReactomeiR-DME-2161541. Abacavir metabolism.
R-DME-5365859. RA biosynthesis pathway.
R-DME-71384. Ethanol oxidation.
SABIO-RKP46415.

Miscellaneous databases

GenomeRNAii41311.
PROiP46415.

Gene expression databases

BgeeiP46415.
GenevisibleiP46415. DM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Drosophila melanogaster glutathione-dependent formaldehyde dehydrogenase/octanol dehydrogenase gene (class III alcohol dehydrogenase). Evolutionary pathway of the alcohol dehydrogenase genes."
    Luque T., Atrian S., Danielsson O., Joernvall H., Gonzalez-Duarte R.
    Eur. J. Biochem. 225:985-993(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo and Ovary.

Entry informationi

Entry nameiADHX_DROME
AccessioniPrimary (citable) accession number: P46415
Secondary accession number(s): Q9VGV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.