ID   I1IX46_BRADI            Unreviewed;      1016 AA.
AC   I1IX46;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=100838957 {ECO:0000313|EnsemblPlants:KQJ82288};
GN   ORFNames=BRADI_5g08230v3 {ECO:0000313|EMBL:KQJ82288.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ82288.1};
RN   [1] {ECO:0000313|EMBL:KQJ82288.1, ECO:0000313|EnsemblPlants:KQJ82288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ82288.1,
RC   ECO:0000313|EnsemblPlants:KQJ82288};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ82288.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ82288.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ82288}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ82288};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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   EMBL; CM000884; KQJ82288.1; -; Genomic_DNA.
DR   RefSeq; XP_003579622.1; XM_003579574.3.
DR   AlphaFoldDB; I1IX46; -.
DR   STRING; 15368.I1IX46; -.
DR   EnsemblPlants; KQJ82288; KQJ82288; BRADI_5g08230v3.
DR   GeneID; 100838957; -.
DR   Gramene; KQJ82288; KQJ82288; BRADI_5g08230v3.
DR   KEGG; bdi:100838957; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; I1IX46; -.
DR   OMA; SFCGQGV; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000008810; Chromosome 5.
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:UP000008810};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          631..844
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1016 AA;  115333 MW;  2F2C594950E2A97E CRC64;
     MGWFRAASGL ARVALRRNLS RVPASPFAGP APRYFHSTRP RRFAAPEPRA VPLSRLTDSF
     LDGTSSVYLE ELQRAWEADP NSVDESWDNF FRNFVGQAST SPGISGQTIQ ESMRLLLLVR
     AYQVSGHLKA KLDPLGLEER PVPDVLDPAF YGFSEADLDR EFFLGVWKMA GFLSDNRPVQ
     TLRSVVERLE QAYCGTIGYE YMHIPDREKC NWLRERIETV NPREYTYDRR QVMLDRLIWS
     TQFENFLAQK WTTAKRFGLE GAETLIPGMK EMFDRAADLG VESIVIGMPH RGRLNVLGNV
     VRKPLRQIFS EFSGGTKPVN EGEGLYTGTG DVKYHLGTSY DRPTRGGKHI HLSLVANPSH
     LEAVDPVVAG KTRAKQYYSN DLDRTKNLGV LLHGDGSFSG QGVVYETLHL SALPNYSTGG
     TIHIVVNNQV AFTTDPLSGR SSQYCTDVAK ALDAPIFHVN GDDLEAVVHT CELAAEWRQT
     FHSDVVVDIV CYRRFGHNEI DEPSFTQPKM YKVIRNHPSA LEIYQKQMLE SGKLSKEDID
     KLHTKVNTIL NEEFKKSKDD IPNKRDWLSA YWTGFKSPEQ ISRVRNTGVK PEILKRVGEA
     MTTLPENFKP HRAVKKIFDL RRQMIETGEG IDWAVGEALA FATLIIEGNH VRLSGQDVER
     GTFSHRHSVV HDQETGQHYC PLDNLVMNQN EELFTVSNSS LSEFAVLGFE LGYSMENPNS
     LVLWEAQFGD FSNGAQVIFD QFISSGEAKW LRQSGLVVCL PHGYDGQGPE HSSARMERFL
     QMSDDNPYVI PEMDSTTRKQ IQQCNLQVVN VTTPANYFHV LRRQIHRDFR KPLIVMSPKN
     LLRHKECKSS LSEFDDVAGH PGFDKQGTRF KRLIKDRNDH KDLEEGINRL VLCSGKVYYE
     LDEERKKSDR NDVAICRVEQ LCPFPYDLIQ RELKRYPNAE IVWCQEEPMN MGAYTYINPR
     LLTAMRALGR GTIEDIKYAG RAPSAATATG FYSVHGQEQT ELVQKALQRD PIKCPF
//