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UniProtKB/Swiss-Prot entry P46415


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADHX_DROME
Primary accession number P46415
Secondary accession number Q9VGV2
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 70)
Name and origin of the protein
Protein name Alcohol dehydrogenase class-3
Synonyms EC 1.1.1.1
Alcohol dehydrogenase class-III
S-(hydroxymethyl)glutathione dehydrogenase
EC 1.1.1.284
Glutathione-dependent formaldehyde dehydrogenase
GSH-FDH
FALDH
FDH
EC 1.1.1.-
Octanol dehydrogenase
EC 1.1.1.73
Gene name
Name: Fdh
Synonyms: gfd, ODH
ORFNames: CG6598
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7957234 [NCBI, ExPASy, EBI, Israel, Japan]
Luque T., Atrian S., Danielsson O., Joernvall H., Gonzalez-Duarte R.;
"Structure of the Drosophila melanogaster glutathione-dependent formaldehyde dehydrogenase/octanol dehydrogenase gene (class III alcohol dehydrogenase). Evolutionary pathway of the alcohol dehydrogenase genes.";
Eur. J. Biochem. 225:985-993(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8197167 [NCBI, ExPASy, EBI, Israel, Japan]
Danielsson O., Atrian S., Luque T., Hjelmqvist L., Gonzalez-Duarte R., Joernvall H.;
"Fundamental molecular differences between alcohol dehydrogenase classes.";
Proc. Natl. Acad. Sci. U.S.A. 91:4980-4984(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo, and Ovary;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U07799; AAA57187.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07641; AAB02520.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF54571.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY089518; AAL90256.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY089615; AAL90353.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S51357; S51357.
RefSeq NP_524310.1; -.
UniGene Dm.1782
3D structure databases
HSSP P11766; 1M6H. [HSSP ENTRY / PDB]
SMR P46415; 7-378.
ModBase P46415.
Protein-protein interaction databases
DIP DIP:23839N; -.
IntAct P46415; -.
Organism-specific databases
FlyBase FBgn0011768; Fdh.
Gene expression databases
ArrayExpress P46415; -.
GermOnline CG6598; Drosophila melanogaster.
Ontologies
GO
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from direct assay from FlyBase).
GO:0004552; Molecular function: octanol dehydrogenase activity (inferred from direct assay from FlyBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0051903; Molecular function: S-(hydroxymethyl)glutathione dehydrogenase activity (inferred from direct assay from FlyBase).
GO:0006066; Biological process: cellular alcohol metabolic process (inferred by curator from FlyBase).
QuickGo view.
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 of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02818; adh_III_F_hyde; 1.
PROSITE PS00059; ADH_ZINC; 1.
BLOCKS P46415.
Genome annotation databases
Ensembl CG6598; Drosophila melanogaster. [Contig view]
GeneID 41311; -.
KEGG dme:Dmel_CG6598; -.
NMPDR fig|7227.3.peg.12145; -.
Phylogenomic databases
HOGENOM P46415; -.
Other
ProtoNet P46415.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (Probable). 
CHAIN   2   379  378     Alcohol dehydrogenase class-3. PRO_0000160769
METAL   48    48        Zinc 1; catalytic (By similarity). 
METAL   70    70        Zinc 1; catalytic (By similarity). 
METAL   100   100        Zinc 2 (By similarity). 
METAL   103   103        Zinc 2 (By similarity). 
METAL   106   106        Zinc 2 (By similarity). 
METAL   114   114        Zinc 2 (By similarity). 
METAL   177   177        Zinc 1; catalytic (By similarity). 
MOD_RES   2     2        N-acetylserine (Probable). 
Sequence information
Length: 379 AA [This is the length of the unprocessed precursor] Molecular weight: 40389 Da [This is the MW of the unprocessed precursor] CRC64: 7F382E10BFACAAC1 [This is a checksum on the sequence]
        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 

P46415 in FASTA format

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