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Q9VA02

- DHTK1_DROME

UniProt

Q9VA02 - DHTK1_DROME

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Protein

Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial

Gene

CG1544

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.By similarity

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
  2. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. generation of precursor metabolites and energy Source: UniProtKB
  2. glycolytic process Source: UniProtKB-KW
  3. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial (EC:1.2.4.2)
Gene namesi
ORF Names:CG1544
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039827. CG1544.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 919Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrialPRO_0000307943
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PaxDbiQ9VA02.

Expressioni

Gene expression databases

BgeeiQ9VA02.
ExpressionAtlasiQ9VA02. differential.

Interactioni

Protein-protein interaction databases

BioGridi68534. 4 interactions.
IntActiQ9VA02. 1 interaction.
MINTiMINT-940711.

Structurei

3D structure databases

ProteinModelPortaliQ9VA02.
SMRiQ9VA02. Positions 54-917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
InParanoidiQ9VA02.
KOiK15791.
OMAiLCSGKHY.
OrthoDBiEOG7CZK4Z.
PhylomeDBiQ9VA02.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9VA02-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRYLALSEA GIAKLPRPQS RCYHSEKGVW GYKPIAQREF QVAEDVRASR
60 70 80 90 100
NSQANVYRFV EAFRQHGHKL AAVNPISIRT SQQELQELSP AFYGLQTQEP
110 120 130 140 150
VRTDGLLSGP QVAHNVAQLE QLLKDIYCGR STSAEFSYVE DIEEREWLAR
160 170 180 190 200
NFETLDQQQL GKSERCEIAE LLIKSQAWDN FMALKFPTVK RYGGEGAESM
210 220 230 240 250
LAFFWQLLRD SVQANIEHVV LAMPHRGRTP LQAALLNMRP AKVFRKLSGA
260 270 280 290 300
SEFSEDIEAM SDVISHFHVS EQLKILGKKL SFSMVRNPSH LEAANPVAMG
310 320 330 340 350
KTRSKQQARG EGAFGDGSQP FGEHVLNVIL HGDAAFAGQG INQECLNMAY
360 370 380 390 400
VPHFEVGGSL HLIVNNQVGF TTPGDRGRST AYTSDLAKSI QAPVFHVNGD
410 420 430 440 450
DPEALARVTS LAFRYQREFR KDIFIDLNCF RRWGHNELDD PTFTNPLVYK
460 470 480 490 500
IVHQRESVPD LYAQQLAKEQ VLSESKAKEM RDEYMKYLGE ELALAPAYQP
510 520 530 540 550
PPSYFEKQWT NFQLAPSKEL TYWDTGLDYS LLHYIGQQSV TFPEDFNIHP
560 570 580 590 600
HLLKTHVNAR LKKLENGVKI DWSTAEALAI GSLMYQGHNV RISGEDVGRG
610 620 630 640 650
TFSHRHAMLV DQQTNEMFIP LNSMEGGNGG KLELAHSILS EEAVLGFEYG
660 670 680 690 700
MAIDNPNNLI IWEAQFGDFA NGAQIIIDTF IVSGETKWME SNALVMLLPH
710 720 730 740 750
GYDGAASEHS SCRIERFLQL CDSKETSADG DSVNVHIVNP TTPAQYYHVL
760 770 780 790 800
RRQLARNFRK PLVVVAPKTL LRLPAATSTH EDFQPGTLFH NVLGDTIAKP
810 820 830 840 850
EQVRKVILCS GKHYYTLAEE REKRQAYDTA ILRLESLCPF PIQELQAQLA
860 870 880 890 900
QYGNVQSFVW SQEEHRNMGA WTFVRPRFEN LIGQQLHYCG RCEAPTPATG
910
IGKVHKREVD EIVAAPFEL
Length:919
Mass (Da):103,635
Last modified:March 1, 2003 - v2
Checksum:i064A1E1034DE5E0E
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481S → G in AAN71328. (PubMed:12537569)Curated
Sequence conflicti913 – 9131V → D in AAN71328. (PubMed:12537569)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF57126.2.
AY118301 mRNA. Translation: AAM48330.1. Different initiation.
BT001573 mRNA. Translation: AAN71328.1.
RefSeqiNP_651849.1. NM_143592.2.
UniGeneiDm.10912.

Genome annotation databases

EnsemblMetazoaiFBtr0085755; FBpp0085117; FBgn0039827.
GeneIDi43689.
KEGGidme:Dmel_CG1544.
UCSCiCG1544-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF57126.2 .
AY118301 mRNA. Translation: AAM48330.1 . Different initiation.
BT001573 mRNA. Translation: AAN71328.1 .
RefSeqi NP_651849.1. NM_143592.2.
UniGenei Dm.10912.

3D structure databases

ProteinModelPortali Q9VA02.
SMRi Q9VA02. Positions 54-917.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68534. 4 interactions.
IntActi Q9VA02. 1 interaction.
MINTi MINT-940711.

Proteomic databases

PaxDbi Q9VA02.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085755 ; FBpp0085117 ; FBgn0039827 .
GeneIDi 43689.
KEGGi dme:Dmel_CG1544.
UCSCi CG1544-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0039827. CG1544.

Phylogenomic databases

eggNOGi COG0567.
GeneTreei ENSGT00530000063092.
InParanoidi Q9VA02.
KOi K15791.
OMAi LCSGKHY.
OrthoDBi EOG7CZK4Z.
PhylomeDBi Q9VA02.

Miscellaneous databases

GenomeRNAii 43689.
NextBioi 835260.
PROi Q9VA02.

Gene expression databases

Bgeei Q9VA02.
ExpressionAtlasi Q9VA02. differential.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo and Head.

Entry informationi

Entry nameiDHTK1_DROME
AccessioniPrimary (citable) accession number: Q9VA02
Secondary accession number(s): Q8IGV6, Q8MT95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3