Reviewed, UniProtKB/Swiss-Prot Q9VA02 (DHTK1_DROME)

Names and origin

Protein names

Recommended name:
    Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial
    EC=1.2.4.2

Gene names

ORF Names:

CG1544

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	919 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VRJ8	1	EBI-166909,EBI-134271

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 919		Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial		PRO_0000307943
Experimental info
	Sequence conflict	248	1	S → G in AAN71328. Ref.3
	Sequence conflict	913	1	V → D in AAN71328. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9VA02-1 [UniParc]. Last modified March 1, 2003. Version 2. Checksum: 064A1E1034DE5E0E	FASTA	919	103,635
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo and Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF57126.2. AY118301 mRNA. Translation: AAM48330.1. Different initiation. BT001573 mRNA. Translation: AAN71328.1.
RefSeq	NP_651849.1.
UniGene	Dm.10912
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VA02. 5 interactions.
STRING	Q9VA02.
Genome annotation databases
Ensembl	FBtr0085755; FBpp0085117; FBgn0039827; Drosophila melanogaster. [Genome view]
GeneID	43689.
UCSC	CG1544-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0039827. CG1544.
Phylogenomic databases
OMA	MIRNFRK.
Enzyme and pathway databases
BRENDA	1.2.4.2. 48.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	835260.

Entry information

Entry name

DHTK1_DROME

Accession

Primary (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:	November 3, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project