ID   DHTK1_DICDI             Reviewed;         900 AA.
AC   Q54VG0;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial;
DE            EC=1.2.4.2;
DE   AltName: Full=Oxoglutarate dehydrogenase A;
DE   Flags: Precursor;
GN   Name=odhA; ORFNames=DDB_G0280353;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, 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}.
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DR   EMBL; AAFI02000035; EAL67403.1; -; Genomic_DNA.
DR   RefSeq; XP_641395.1; XM_636303.1.
DR   AlphaFoldDB; Q54VG0; -.
DR   SMR; Q54VG0; -.
DR   STRING; 44689.Q54VG0; -.
DR   PaxDb; 44689-DDB0230197; -.
DR   EnsemblProtists; EAL67403; EAL67403; DDB_G0280353.
DR   GeneID; 8622529; -.
DR   KEGG; ddi:DDB_G0280353; -.
DR   dictyBase; DDB_G0280353; odhA.
DR   eggNOG; KOG0451; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; Q54VG0; -.
DR   OMA; TPAQYYH; -.
DR   PhylomeDB; Q54VG0; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:Q54VG0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IC:dictyBase.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 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   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..900
FT                   /note="Probable 2-oxoglutarate dehydrogenase E1 component
FT                   DHKTD1 homolog, mitochondrial"
FT                   /id="PRO_0000388782"
SQ   SEQUENCE   900 AA;  101831 MW;  F2F2A86C9191EF98 CRC64;
     MIGLRSISKN KQTINSISKS FYCTSSPSSS SVKLSVTRLI DGYRAHGHLA ANIDPLARME
     RIRSQLLDLD RYNLVKGQSI PSTIDLINQD LTNLDQVVSF LENAYCNDVT AQFDHIESIE
     EKAWLYEKFE QLQHQNPSKS EKINILKNLI KSEIFDQFMQ KKFPTFKRYG LEGNESMMVS
     CDSIFRESAK NQLKNVVIGM PHRGRLNLLV QMCNYPAKDF FWKVKGNSEF SEGILGVGDV
     TSHIAVSTDL QFNNNKESVH VSLIHNPSHL EAVDPVAAGK TRAKQFYEKN EGGSESLCLM
     LHGDAAVAGQ GVVTETLQLS QLSGFNIGGC VHVIVNNQIG FTTVPTNGRS NRYSSDIGKF
     IGAPIIVVNS QSPEQVEKVS RLAVEYRQKF KKDIIIDLIG WRKFGHNEVD EPSFTQPTMY
     QNIRKRQSIP QKYATQIISQ GIFSEQELLE FTQKEQAILE EQFQLSTPEN FKYSPMDHLQ
     GKWSGLIQSK HIADDSKLDT GYSVEELSEI ANDSVKVPSD FQVHQRLLRS FSNARLEKLK
     QNQADWATAE SMAVGSLMKQ GYNVRISGQD VGRGTFSQRH FNLTEQNSDR IYQPLNNMGA
     KGELDVVNSN LSEFAVLCYE YGYSLESPDT LPIWEAQFGD FINGAQIAID QFVTSGESKW
     LRQSGIVILL PHGFDGAGPE HSSCRIERFL QLSDTEAVNV KDDTLINQET NFYFINPSTP
     ANYFHALRRQ MIRNYRKPLI VAGPKVLLRH PNCFSTLNEM APGTHFQTVL SDPDTINNAS
     TIKRVIFCSG KVFYDLQEER KAKNFNDVAI IRLEQIAPFP YQRIQEEINR YSNATKFAWV
     QEEQQNGGCW SFVEPRFKQR YPQTSQIKYI GRPPLAASAI GISSIHKKEV SQLLIDAFNF
//