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UniProtKB/Swiss-Prot entry Q9W265


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

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Entry information
Entry name HOT_DROME
Primary accession number Q9W265
Secondary accession number Q8SX03
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial [Precursor]
Synonyms HOT
EC 1.1.99.24
Gene name
Name: T3dh
ORFNames: CG3425
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 2: Evidence at transcript level;
References
[1]
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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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
AE013599; AAF46832.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY094924; AAM11277.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_477209.2; -.
UniGene Dm.33441
3D structure databases
ModBase Q9W265.
Organism-specific databases
FlyBase FBgn0017482; T3dh.
Gene expression databases
ArrayExpress Q9W265; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0047988; Molecular function: hydroxyacid-oxoacid transhydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0015993; Biological process: molecular hydrogen transport (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001670; Fe_AlcDHase.
Graphical view of domain structure.
Pfam PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.
PROSITE PS00913; ADH_IRON_1; FALSE_NEG.
PS00060; ADH_IRON_2; FALSE_NEG.
BLOCKS Q9W265.
Genome annotation databases
Ensembl CG3425; Drosophila melanogaster. [Contig view]
GeneID 37551; -.
KEGG dme:Dmel_CG3425; -.
NMPDR fig|7227.3.peg.6828; -.
Other
ProtoNet Q9W265.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Mitochondrion; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   464        Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial. PRO_0000323005
CONFLICT   108   108        R -> L (in Ref. 3; AAM11277). 
Sequence information
Length: 464 AA [This is the length of the unprocessed precursor] Molecular weight: 50018 Da [This is the MW of the unprocessed precursor] CRC64: 2351EA6F02E957CD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRKNVLGLI NTIVANSCKC PAHSHNYGSA APTASQTGRM EYAFEMSAST VRFGPGVSAE 

        70         80         90        100        110        120 
VGADLRNLGA RKVCLVTDKN VVQLPSVKVA LDSLARNGIN YEVYDETRVE PTDGSMWHAV 

       130        140        150        160        170        180 
EFARGKEFDA FLAIGGGSAM DTAKAANLFS SDANAEFLDY VNCPIGRGKE ISVKLKPLIA 

       190        200        210        220        230        240 
MPTTSGTGSE TTGVAIFDYK KLHAKTGISS KFLKPTLAVI DPLHTLSQPQ RVMAFAGFDV 

       250        260        270        280        290        300 
FCHALESFTA VDYRERGLAP SDPSLRPTYQ GRNPVSDVWA RFALETIRKN FVNAIYQPDN 

       310        320        330        340        350        360 
LEARSQMHLA STMAGVGFGN AGVHLCHGLS YPISGNVRDY KPKGYSADHA LIPHGLSVVI 

       370        380        390        400        410        420 
SAPAVFEFTA PACPDRHLEA AQLLGAEVRG VEKADAGRLL ADTVRGFMQR AGIENGLREL 

       430        440        450        460 
GFSSSDIPAL VEGTLPQERI TKLAPRAQTQ ENLSQLFEKS MEVY 

Q9W265 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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