ID A0A2K6UMJ4_SAIBB Unreviewed; 1038 AA.
AC A0A2K6UMJ4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 Name=OGDH {ECO:0000313|Ensembl:ENSSBOP00000033149.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000033149.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000033149.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR RefSeq; XP_010339664.1; XM_010341362.1.
DR AlphaFoldDB; A0A2K6UMJ4; -.
DR STRING; 39432.ENSSBOP00000033149; -.
DR Ensembl; ENSSBOT00000050060.1; ENSSBOP00000033149.1; ENSSBOG00000032539.1.
DR GeneID; 101030121; -.
DR CTD; 4967; -.
DR GeneTree; ENSGT00950000183125; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IEA:Ensembl.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:Ensembl.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR GO; GO:0021695; P:cerebellar cortex development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
DR GO; GO:0021794; P:thalamus development; IEA:Ensembl.
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:UP000233220};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 666..880
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1038 AA; 117661 MW; 1EB2F940F353EE48 CRC64;
MFHLRTCATK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLDLAVFKER
LRMLTVGGFY GLDESDLDKV FHLPTTTFIG GQESALPLRE IIRRLEMAYC QHIGVEFMFI
NDLEQCQWIR QKFETPGIMQ FTNEEKRTLL ARLVRSTRFE EFLQRKWSSE KRFGLEGCEV
LIPALKTIID KSSENGVDYV IMGMPHRGRL NVLANVIRKE LEQIFCQFDS KLEAADEGSG
DVKYHLGMYH RRINRVTDRN ITLSLVANPS HLEAADPVVM GKTKAEQFYC GDTEGKKVMS
ILLHGDAAFA GQGIVYETFH LSDLPSYTTH GTVHVVVNNQ IGFTTDPRMA RSSPYPTDVA
RVVNAPIFHV NSDDPEAVMY VCKVAAEWRS TFHKDVVVDL VCYRRNGHNE MDEPMFTQPL
MYKQIRKQKP VLQKYAELLV SQGVVNQPEY EEEISKYDKI CEEAFARSKD EKILHIKHWL
DSPWPGFFTL DGQPRSMSCP STGLTEDILT HIGNVASSVP VENFTIHGGL SRILKTRGEM
VKNRTVDWAL AEYMAFGSLL KEGIHIRLSG QDVERGTFSH RHHVLHDQNV DKRTCIPMNH
LWPNQAPYTV CNSSLSEYGV LGFELGFAMA SPNALVLWEA QFGDFHNTAQ CIIDQFICPG
QAKWVRQNGI VLLLPHGMEG MGPEHSSARP ERFLQMCNDD PDVLPDLQEA NFDINQLYDC
NWVVVNCSTP GNFFHVLRRQ ILLPFRKPLI IFTPKSLLRH PEARSSFDEM LPGTHFQRVI
PEDGPAAQNP ENVKRLLFCT GKVYYDLTRE RKARDMVGQV AITRIEQLSP FPFDLLLKEV
QKYPNAELAW CQEEHKNQGY YDYVKPRLRT TISRAKPVWY AGRDPAAAPA TGNKKTHLTE
LQRLLDTAFD LDVFKNLS
//
