Reviewed, UniProtKB/Swiss-Prot P46415 (ADHX_DROME)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase class-3
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase class-III
    S-(hydroxymethyl)glutathione dehydrogenase
    EC=1.1.1.284
    Glutathione-dependent formaldehyde dehydrogenase
      Short name=GSH-FDH
      Short name=FALDH
      Short name=FDH
    EC=1.1.1.-
    Octanol dehydrogenase
    EC=1.1.1.73

Gene names

Name:	Fdh
Synonyms:	gfd, ODH
ORF Names:	CG6598

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 activity	An alcohol + NAD(+) = an aldehyde or ketone + NADH. S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H. 1-octanol + NAD(+) = 1-octanal + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular alcohol metabolic process Ref.2 Inferred by curator. Source: FlyBase oxidation reduction Inferred from electronic annotation. Source: InterPro
Molecular function	S-(hydroxymethyl)glutathione dehydrogenase activity Ref.2 Inferred from electronic annotation. Source: EC alcohol dehydrogenase activity Ref.2 Inferred from electronic annotation. Source: EC octanol dehydrogenase activity Ref.2 Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MED28	Q9VBQ9	1	EBI-192142,EBI-174566

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 379	378	Alcohol dehydrogenase class-3		PRO_0000160769
Sites
	Metal binding	48	1	Zinc 1; catalytic By similarity
	Metal binding	70	1	Zinc 1; catalytic By similarity
	Metal binding	100	1	Zinc 2 By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	114	1	Zinc 2 By similarity
	Metal binding	177	1	Zinc 1; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Probable

Sequences

	Sequence		Length	Mass (Da)
	P46415-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7F382E10BFACAAC1	FASTA	379	40,389
	10 20 30 40 50 60 MSATEGKVIT CKAAVAWEAK KPLVIEDIEV APPKAHEVRI KITATGVCHT DAFTLSGADP 70 80 90 100 110 120 EGLFPVVLGH EGAGIVESVG EGVTNFKAGD HVIALYIPQC NECKFCKSGK TNLCQKIRLT 130 140 150 160 170 180 QGAGVMPEGT SRLSCKGQQL FHFMGTSTFA EYTVVADISL TKINEKAPLE KVCLLGCGIS 190 200 210 220 230 240 TGYGAALNTA KVEAGSTCAV WGLGAVGLAV GLGCKKAGAG KIYGIDINPD KFELAKKFGF 250 260 270 280 290 300 TDFVNPKDVA DKGSIQNYLI DLTDGGFDYT FECIGNVNTM RSALEATHKG WGTSVVIGVA 310 320 330 340 350 360 GAGQEISTRP FQLVVGRVWK GSAFGGWRSV SDVPKLVEDY LKKDLLVDEF ITHELPLSQI 370 NEAFDLMHKG ESIRSIIKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7957234] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Fundamental molecular differences between alcohol dehydrogenase classes." Danielsson O., Atrian S., Luque T., Hjelmqvist L., Gonzalez-Duarte R., Joernvall H. Proc. Natl. Acad. Sci. U.S.A. 91:4980-4984(1994) [PubMed: 8197167] [Abstract] 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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo and Ovary.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	S51357.
RefSeq	NP_524310.1.
UniGene	Dm.1782
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
SMR	P46415. Positions 7-378.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:23839N.
IntAct	P46415.
Genome annotation databases
Ensembl	CG6598. Drosophila melanogaster. [Contig view]
GeneID	41311.
KEGG	dme:Dmel_CG6598.
NMPDR	fig|7227.3.peg.12145.
Organism-specific databases
FlyBase	FBgn0011768. Fdh.
Phylogenomic databases
HOGENOM	P46415.
Gene expression databases
ArrayExpress	P46415.
GermOnline	CG6598. Drosophila melanogaster.
Family and domain databases
InterPro	IPR014183. AlcDHase_3. IPR013154. AlcDHase_GroES-like. IPR002085. AlcDHase_SF_Zn. IPR013149. AlcDHase_Zn-bd. IPR002328. AlcDHase_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR02818. adh_III_F_hyde. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	823264.

Entry information

Entry name

ADHX_DROME

Accession

Primary (citable) accession number: P46415
Secondary accession number(s): Q9VGV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project