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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: 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

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: GO_Central
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
  2. mitochondrion Source: GO_Central
  3. oxoglutarate dehydrogenase complex Source: GO_Central
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. 2 interactions.
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.
OMAiEHSSCRM.
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi68534. 4 interactions.
IntActiQ9VA02. 2 interactions.
MINTiMINT-940711.

Proteomic databases

PaxDbiQ9VA02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

FlyBaseiFBgn0039827. CG1544.

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
InParanoidiQ9VA02.
KOiK15791.
OMAiEHSSCRM.
OrthoDBiEOG7CZK4Z.
PhylomeDBiQ9VA02.

Miscellaneous databases

GenomeRNAii43689.
NextBioi835260.
PROiQ9VA02.

Gene expression databases

BgeeiQ9VA02.
ExpressionAtlasiQ9VA02. differential.

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.
ProtoNetiSearch...

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: February 4, 2015
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.