ID   Q6C3M8_YARLI            Unreviewed;      1004 AA.
AC   Q6C3M8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 2.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN   ORFNames=YALI0_E33517g {ECO:0000313|EMBL:CAG80338.2};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG80338.2, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG80338.2, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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). {ECO:0000256|ARBA:ARBA00037426}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382131; CAG80338.2; -; Genomic_DNA.
DR   RefSeq; XP_504734.2; XM_504734.2.
DR   AlphaFoldDB; Q6C3M8; -.
DR   STRING; 284591.Q6C3M8; -.
DR   EnsemblFungi; CAG80338; CAG80338; YALI0_E33517g.
DR   GeneID; 2912855; -.
DR   KEGG; yli:YALI0E33517g; -.
DR   VEuPathDB; FungiDB:YALI0_E33517g; -.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; Q6C3M8; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; IPR032106; 2-oxogl_dehyd_N.
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; PF16078; 2-oxogl_dehyd_N; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          632..842
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          81..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  113726 MW;  BCF7053523827F21 CRC64;
     MLRHALLKRT PVLPRLTSRK AFVPLIQKRK YSDDVFLTTN AANYIDEMYA AWKDDPKSVH
     VSWQSYFKNL DGGLPADKAF SAPPTIVPSP SGGVPTPAAP SGAPSDITNH MKAQLLVRAY
     QVRGHTKAKI DPLGISFGSD KNKKPPKELT LEFYGWTDKD LDTEITLGPG ILPRFVENGK
     NKRTLREIIM DCERIYCGSY GVEYIHIPSR EECEWIRDRV ETPKPYNYTP DQKRRMLDRL
     IWANLFETFL ASKFPNDKRF GLEGAETVVV GMKTLIDRSV DAGIEDIVIG MPHRGRLNML
     SNVVRKPNES IFAEFQGSAV FDEGSGDVKY HLGANYQRPT PSGKKVNLSL VANPSHLEAE
     DPVVLGKTRA IQHMKHDVGT FDKAMGVLMH GDAAFAGQGV VYETMGMHSL PAYSTGGTIH
     IIVNNQIGFT TDPRFSRSTP YPSDLAKSID APIFHVNADD MEAVDFIFNL AADWRATFKS
     DVIIDLVCYR KFGHNETDQP SFTQPLMYKK IADKPNPLDI YVDKLLKEKT FTKEDIEEHK
     QWVWGMLEES FKKSKDYVPH QKEWLASPWD DFKTPKELAT EILPHLPTSV EEKKLKEIGK
     VISSVPEGFT LHRNLKRILS NRGKSVEEGH GIDWSTGEAL AFGTLLEEGH HVRLSGQDVE
     RGTFSQRHAV VHDQVNETTY VPLNHLTKDQ ADFTVSNSHL SEYGVMGFEY GYSLASPEAL
     VIWEAQFGDF ANTAQVIIDQ FIASAETKWS QRSGLVLSLP HGYDGQGPEH SSGRIERYLL
     LGNEDPLHFP SPDKLERQHQ DCNIQIAYPT TPANIFHLYR RQMHRAFRKP LACFFSKNLL
     RNPMAKSDLS EFVGESHFQW VIEDDQHGKT INNKEGIERV LFCSGQVWTA LFKRREDLAD
     KKTAIIRIEQ LHPFPWEQVR ELLDSYPNLK DICWAQEEPL NAGAWVHIQP RMYTTFQATK
     NHKHAHIRYA GRKPSASVAA GTKKLHLAEE EALLKQAFQQ EDKA
//