ID M1CNJ1_SOLTU Unreviewed; 1020 AA.
AC M1CNJ1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 Name=102591883 {ECO:0000313|EnsemblPlants:PGSC0003DMT400071319};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400071319, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400071319}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400071319};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 RefSeq; XP_006365716.1; XM_006365654.2.
DR RefSeq; XP_006365717.1; XM_006365655.2.
DR RefSeq; XP_006365718.1; XM_006365656.2.
DR RefSeq; XP_015160050.1; XM_015304564.1.
DR AlphaFoldDB; M1CNJ1; -.
DR STRING; 4113.M1CNJ1; -.
DR CarbonylDB; M1CNJ1; -.
DR PaxDb; 4113-PGSC0003DMT400071319; -.
DR EnsemblPlants; PGSC0003DMT400071318; PGSC0003DMT400071318; PGSC0003DMG400027739.
DR EnsemblPlants; PGSC0003DMT400071319; PGSC0003DMT400071319; PGSC0003DMG400027739.
DR GeneID; 102591883; -.
DR Gramene; PGSC0003DMT400071318; PGSC0003DMT400071318; PGSC0003DMG400027739.
DR Gramene; PGSC0003DMT400071319; PGSC0003DMT400071319; PGSC0003DMG400027739.
DR KEGG; sot:102591883; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; M1CNJ1; -.
DR OMA; IRIRRHN; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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:UP000011115};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 635..848
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1020 AA; 115306 MW; 17C76ABEED4DCA83 CRC64;
MAWFRAGSSV AKLAIRRAVS QGGSYVPRTR IIPSQSRYFH TTVVRPKAQA APVPRPVPLS
KLTDSFLDGT SSVYLEELQR AWEQDPSSVD ESWDNFFRNF TGLAATSPGI SGQTIQESMN
LLLLVRAYQV NGHLKAKLDP LDLEERDIPD VLDPVSYGFT EADLDREFFL GVWRMAGFLS
ENRPVQTLRA ILTRLEQAYC GSIGFEYMHI SDHDKCNWLR ERIETPTPRE YNRERREVIL
DRLMWSTQFE NFLATKWVAA KRFGLEGCET LIPGMKEMFD RSADLGVESI VIGMPHRGRL
NVLGNVVRKP LRQIFSEFTG GTKPADGAGY VGTGDVKYHL GTSYDRPTRG GKRIHLSLVA
NPSHLEAVDP VVIGKTRAKQ YYSNDVDRTK NMGILLHGDG SFAGQGVVYE TLHLSALPNY
TTGGTIHIVV NNQVAFTTDP KAGRSSQYCT DVAKALSAPI FHVNGDDVEG VVHACELAAE
WRQTFHSDVV VDIVCYRRFG HNEIDEPSFT QPKMYQVIRN HPSSLEIYQN KLLQYGQVTK
DDVEKIHNKI NTILNEEFVA SKDYVPQKRD WLSAFWSGFK SPAQLSRVRN TGVKPEILKD
VGKAITSLPD DFKAHRAVKR IFDDRKKMIE TGEGVDWAVG EALAFATLLV EGNHVRLSGQ
DVERGTFSHR HSVIHDQETG AKYCPLDHVM MNQNEEMFTV SNSSLSEFGV LGFELGYSME
NPNSLVLWEA QFGDFANGAQ VIFDQFLSSG EAKWLRQSGL VVLLPHGYDG QGPEHSSARL
ERFLQMSDDN PYVIPDMEPT LRKQIQECNW QVVNVTTPAN YFHVLRRQIH RDFRKPLIVM
SPKNLLRHKD CKSNLSEFDD VQGHPGFDKQ GTRFKRLIKD QNDHSDLEEG IRRLVLCSGK
VYYELDEERK KVEGKDVAIC RVEQLCPFPY DLVQRELKRY PNAEIVWCQE EPMNMGAYQY
IAPRLSTAMK ALDRGNIDDI KYAGRGPSAA TATGFYQVHV KEQTGLVQKA LQQDPINSPV
//
