ID A0A0Q3U162_AMAAE Unreviewed; 1016 AA.
AC A0A0Q3U162;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040429};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041946};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
DE AltName: Full=Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00042799};
GN ORFNames=AAES_18686 {ECO:0000313|EMBL:KQL59712.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL59712.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL59712.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL59712.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQL59712.1}.
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DR EMBL; LMAW01000276; KQL59712.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3U162; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF7; 2-OXOGLUTARATE DEHYDROGENASE COMPLEX COMPONENT E1; 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 Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 646..858
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1016 AA; 115315 MW; 9BE682ECFF533EEC CRC64;
MLNLRTCVAK LRPLTASQTV KTISQHRLAA PRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
MYYAWLENPK SVHKSWDIFF RNANAGAAPG TAYQSPPPLS TSLSTLTQAQ FLGQAQPNVD
KLVEDHLAVQ SLIRAYQVRG HHIAKLDPLG ISCVNFDDAP VTVSSNVGFY GLDESDLDKV
FHLPTTTFIG GNESALPLRE IIRRLEMAYC QHIGVEFMFI NDLEQCQWIR RKFETPGIMQ
FTNEEKRTLL ARLVRSTRFE EXLHRKWSSE KRFGLEGCEV LIPALKTIID KSSEKGVDYV
IMGMPHRGRL NVLANVIRKE LEQIFCQFDS KLEAADEGSG DVKYHLGMYH RRINRVTDRN
ITLSLVANPS HLEAADPVVQ GKTKAEQFYC GDTEGKKVMS ILLHGDAAFA GQGIVYETFH
LXDLPSYTTH GTVHVVVNNQ IGFTTDPRMA RSSPYPTDVA RVVNAPIFHV NADDPEAVVY
VCNVAAEWRS TFHKDVVVDL VCYRRNGHNE MDEPMFTQPL MYKQIRKQKP VLQKYAELLI
SQGVVNQLEY EEEIAKYDKI CEEAHARSKD EKILHIKHWL DSPWPGFFTL DGQPRSMTCP
STGLNEEDLT HIGQVASSVP VEDFTIHGGL SRILKTRGEM VKNRTVDWAL AEYMAFGSLL
KDGIHIRLSG QDVERGTFSH RHHVLHDQNV DKRTCIPMNH LWPSQAPYTV CNSSLSEYGV
LGFELGFAMA SPNALVLWEA QFGDFHNTAQ CIIDQFICPG QAKWVRQNGI VLLLPHGMEG
MGPEHSSARP ERFLQMCNDD PDVFPKLDDF DVRQLYECNW IVVNCSTPAN FFHVLRRQIL
LPFRKPLIIF TPKSLLRHPE ARSSFDDMLP GTHFLRVIPD SGPAAQNPEQ VKRVLFCTGK
VYYDLTRERK ARQMEADVAI TRVEQLSPFP FDLLQREAEK YPAAELVWCQ EEHKNQGYYD
YVKPRLRTTI NRAKPVWYAG REPAAAPATG NKKTHLTELQ RLLDTAFNLD AFKDLS
//
