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
//
