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Q9VA02 (DHTK1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial
EC=1.2.4.2
Gene names
ORF Names:CG1544
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate By similarity.

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Sequence caution

The sequence AAM48330.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 919Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrialPRO_0000307943

Experimental info

Sequence conflict2481S → G in AAN71328. Ref.3
Sequence conflict9131V → D in AAN71328. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9VA02 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: 064A1E1034DE5E0E

FASTA919103,635
        10         20         30         40         50         60 
MLRYLALSEA GIAKLPRPQS RCYHSEKGVW GYKPIAQREF QVAEDVRASR NSQANVYRFV 

        70         80         90        100        110        120 
EAFRQHGHKL AAVNPISIRT SQQELQELSP AFYGLQTQEP VRTDGLLSGP QVAHNVAQLE 

       130        140        150        160        170        180 
QLLKDIYCGR STSAEFSYVE DIEEREWLAR NFETLDQQQL GKSERCEIAE LLIKSQAWDN 

       190        200        210        220        230        240 
FMALKFPTVK RYGGEGAESM LAFFWQLLRD SVQANIEHVV LAMPHRGRTP LQAALLNMRP 

       250        260        270        280        290        300 
AKVFRKLSGA SEFSEDIEAM SDVISHFHVS EQLKILGKKL SFSMVRNPSH LEAANPVAMG 

       310        320        330        340        350        360 
KTRSKQQARG EGAFGDGSQP FGEHVLNVIL HGDAAFAGQG INQECLNMAY VPHFEVGGSL 

       370        380        390        400        410        420 
HLIVNNQVGF TTPGDRGRST AYTSDLAKSI QAPVFHVNGD DPEALARVTS LAFRYQREFR 

       430        440        450        460        470        480 
KDIFIDLNCF RRWGHNELDD PTFTNPLVYK IVHQRESVPD LYAQQLAKEQ VLSESKAKEM 

       490        500        510        520        530        540 
RDEYMKYLGE ELALAPAYQP PPSYFEKQWT NFQLAPSKEL TYWDTGLDYS LLHYIGQQSV 

       550        560        570        580        590        600 
TFPEDFNIHP HLLKTHVNAR LKKLENGVKI DWSTAEALAI GSLMYQGHNV RISGEDVGRG 

       610        620        630        640        650        660 
TFSHRHAMLV DQQTNEMFIP LNSMEGGNGG KLELAHSILS EEAVLGFEYG MAIDNPNNLI 

       670        680        690        700        710        720 
IWEAQFGDFA NGAQIIIDTF IVSGETKWME SNALVMLLPH GYDGAASEHS SCRIERFLQL 

       730        740        750        760        770        780 
CDSKETSADG DSVNVHIVNP TTPAQYYHVL RRQLARNFRK PLVVVAPKTL LRLPAATSTH 

       790        800        810        820        830        840 
EDFQPGTLFH NVLGDTIAKP EQVRKVILCS GKHYYTLAEE REKRQAYDTA ILRLESLCPF 

       850        860        870        880        890        900 
PIQELQAQLA QYGNVQSFVW SQEEHRNMGA WTFVRPRFEN LIGQQLHYCG RCEAPTPATG 

       910 
IGKVHKREVD EIVAAPFEL

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"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 Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014297 Genomic DNA. Translation: AAF57126.2.
AY118301 mRNA. Translation: AAM48330.1. Different initiation.
BT001573 mRNA. Translation: AAN71328.1.
RefSeqNP_651849.1. NM_143592.2.
UniGeneDm.10912.

3D structure databases

ProteinModelPortalQ9VA02.
SMRQ9VA02. Positions 54-917.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VA02. 1 interaction.
MINTMINT-940711.

Proteomic databases

PaxDbQ9VA02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085755; FBpp0085117; FBgn0039827.
GeneID43689.
KEGGdme:Dmel_CG1544.
UCSCCG1544-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0039827. CG1544.

Phylogenomic databases

eggNOGCOG0567.
GeneTreeENSGT00530000063092.
InParanoidQ9VA02.
KOK15791.
OMAEYGISIA.
OrthoDBEOG4NP5JJ.
PhylomeDBQ9VA02.

Gene expression databases

BgeeQ9VA02.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi43689.
NextBio835260.

Entry information

Entry nameDHTK1_DROME
AccessionPrimary (citable) accession number: Q9VA02
Secondary accession number(s): Q8IGV6, Q8MT95
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents