ID   C5DMI7_LACTC            Unreviewed;      1013 AA.
AC   C5DMI7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   OrderedLocusNames=KLTH0G09262g {ECO:0000313|EMBL:CAR24998.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR24998.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR24998.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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}.
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DR   EMBL; CU928171; CAR24998.1; -; Genomic_DNA.
DR   RefSeq; XP_002555435.1; XM_002555389.1.
DR   AlphaFoldDB; C5DMI7; -.
DR   STRING; 559295.C5DMI7; -.
DR   GeneID; 8293712; -.
DR   KEGG; lth:KLTH0G09262g; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; C5DMI7; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000002036; Chromosome G.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; 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:UP000002036};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          646..856
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1013 AA;  114546 MW;  7BFBCDB6A05D95F3 CRC64;
     MLRGISRFSQ QSVAKRALYR SGNQCVRGNW GTRCLATNSS DNFLSTTNAA YIDEMYEAWQ
     KDPTSVHVSW NAYFKNMGNA GIPASSAFVA PPTLVSHHTG AQIPQDMVMG ASGTMDQGIL
     THLKVQLLCR AYQVRGHQKA HIDPLQISFG DDKSKPLPKE LTLEHYGFTE RDLDREITLG
     PGILPRFTRE GKKAMTLREI IAALEKLYCS SYGIEYIHIP SRAQCDWLRE RIEIPQPYHY
     TIDQKRQILD RLTWATSFET FLSTKFPNDK RFGLEGLEGV VPGIKTLIDK SVELGVEDVV
     LGMAHRGRLN VLSNVVRKPN ESIFSEFQGS AAPEEYEGSG DVKYHLGMNY QRPTTSGKYV
     NLSLVANPSH LESQDPVVLG RTRAIMFAKN DLDKYQKAMG VLLHGDAAFA AQGVVYETMG
     FSHLPDYSSG GTIHIITNNQ IGFTTDPRFA RSTPYPSDIA KAIDAPIFHV NANDVEALTF
     IFNLAAEWRA TFHTDAIIDV VGWRKHGHNE TDQPSFTQPL MYQKISKQKS VIDVYTEKLI
     SEGSFTKKDI DEHKQWVWGL FEKAFEKAKD YEPTSREWLT ADWANFKSPK ELATEILPHE
     PTVVQQEKLK EIGKIISSWP EDFEVHRNLK RILTNRGKSI EKGEGIDWST GEALALGSLA
     TEGYHIRVSG EDVERGTFSQ RHAVLHDQKS ERTYTPLQHL SDKQANFTIC NSSLSEYGCM
     GFEYGYSLTS PDFLVMWEAQ FGDFANTGQV IIDQFLAGGE AKWKQRSGLV LSLPHGYDGQ
     GPEHSSGRLE RFLQMANEDP RYFPSEEKLQ RQHQDCNFQV VYPTTPANLF HILRRQQHRQ
     FRKPLILFFS KQLLRHPLAR SKLSDFSDNG FQWIIEDVEH GKSIASKEET KRLVIMSGQV
     YTALHKKRES LGDKNTAFLK VEQLHPFPFA QLRDSLNSYP NLEDIVFCQE EPLNMGSWAY
     AAPRLGTVLK ETDKYKDFEV RFAGRNPSGA VAAGSKALHA AEEEAFLKEV FGQ
//