DHTK1_DROME
ID DHTK1_DROME Reviewed; 919 AA.
AC Q9VA02; Q8IGV6; Q8MT95;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial;
DE EC=1.2.4.2;
DE Flags: Precursor;
GN ORFNames=CG1544;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM48330.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF57126.2; -; Genomic_DNA.
DR EMBL; AY118301; AAM48330.1; ALT_INIT; mRNA.
DR EMBL; BT001573; AAN71328.1; -; mRNA.
DR RefSeq; NP_651849.1; NM_143592.2.
DR AlphaFoldDB; Q9VA02; -.
DR SMR; Q9VA02; -.
DR BioGRID; 68534; 5.
DR IntAct; Q9VA02; 2.
DR STRING; 7227.FBpp0085117; -.
DR PaxDb; Q9VA02; -.
DR PRIDE; Q9VA02; -.
DR EnsemblMetazoa; FBtr0085755; FBpp0085117; FBgn0039827.
DR GeneID; 43689; -.
DR KEGG; dme:Dmel_CG1544; -.
DR UCSC; CG1544-RA; d. melanogaster.
DR FlyBase; FBgn0039827; CG1544.
DR VEuPathDB; VectorBase:FBgn0039827; -.
DR eggNOG; KOG0451; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; Q9VA02; -.
DR OMA; GMAIDNP; -.
DR OrthoDB; 134699at2759; -.
DR PhylomeDB; Q9VA02; -.
DR Reactome; R-DME-389661; Glyoxylate metabolism and glycine degradation.
DR BioGRID-ORCS; 43689; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43689; -.
DR PRO; PR:Q9VA02; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039827; Expressed in embryonic/larval hemocyte (Drosophila) and 16 other tissues.
DR ExpressionAtlas; Q9VA02; baseline and differential.
DR Genevisible; Q9VA02; DM.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.50.11610; -; 1.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 2: Evidence at transcript level;
KW Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome;
KW Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..919
FT /note="Probable 2-oxoglutarate dehydrogenase E1 component
FT DHKTD1 homolog, mitochondrial"
FT /id="PRO_0000307943"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 248
FT /note="S -> G (in Ref. 3; AAN71328)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="V -> D (in Ref. 3; AAN71328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 103635 MW; 064A1E1034DE5E0E CRC64;
MLRYLALSEA GIAKLPRPQS RCYHSEKGVW GYKPIAQREF QVAEDVRASR NSQANVYRFV
EAFRQHGHKL AAVNPISIRT SQQELQELSP AFYGLQTQEP VRTDGLLSGP QVAHNVAQLE
QLLKDIYCGR STSAEFSYVE DIEEREWLAR NFETLDQQQL GKSERCEIAE LLIKSQAWDN
FMALKFPTVK RYGGEGAESM LAFFWQLLRD SVQANIEHVV LAMPHRGRTP LQAALLNMRP
AKVFRKLSGA SEFSEDIEAM SDVISHFHVS EQLKILGKKL SFSMVRNPSH LEAANPVAMG
KTRSKQQARG EGAFGDGSQP FGEHVLNVIL HGDAAFAGQG INQECLNMAY VPHFEVGGSL
HLIVNNQVGF TTPGDRGRST AYTSDLAKSI QAPVFHVNGD DPEALARVTS LAFRYQREFR
KDIFIDLNCF RRWGHNELDD PTFTNPLVYK IVHQRESVPD LYAQQLAKEQ VLSESKAKEM
RDEYMKYLGE ELALAPAYQP PPSYFEKQWT NFQLAPSKEL TYWDTGLDYS LLHYIGQQSV
TFPEDFNIHP HLLKTHVNAR LKKLENGVKI DWSTAEALAI GSLMYQGHNV RISGEDVGRG
TFSHRHAMLV DQQTNEMFIP LNSMEGGNGG KLELAHSILS EEAVLGFEYG MAIDNPNNLI
IWEAQFGDFA NGAQIIIDTF IVSGETKWME SNALVMLLPH GYDGAASEHS SCRIERFLQL
CDSKETSADG DSVNVHIVNP TTPAQYYHVL RRQLARNFRK PLVVVAPKTL LRLPAATSTH
EDFQPGTLFH NVLGDTIAKP EQVRKVILCS GKHYYTLAEE REKRQAYDTA ILRLESLCPF
PIQELQAQLA QYGNVQSFVW SQEEHRNMGA WTFVRPRFEN LIGQQLHYCG RCEAPTPATG
IGKVHKREVD EIVAAPFEL
