ID G3TBV2_LOXAF Unreviewed; 1034 AA.
AC G3TBV2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:ENSLAFP00000011489.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000011489.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000011489.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011489.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000011489.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011489.2};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; G3TBV2; -.
DR STRING; 9785.ENSLAFP00000011489; -.
DR Ensembl; ENSLAFT00000013725.2; ENSLAFP00000011489.2; ENSLAFG00000013723.2.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; G3TBV2; -.
DR OMA; RDSYCRT; -.
DR TreeFam; TF300695; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:UP000007646};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 662..876
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1034 AA; 117367 MW; 30F7B573321E2108 CRC64;
MFHLRTCAAK LRPLTASQTV KTFAQNRPAA ARTFQQIRCY TAPVAAEPFL SGTSSNYVEE
MYYAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLSTIARA QSLVEAQPNV
DKLVEDHLAV QSLIRAYQVR GHHIAKLDPL GISCVNFDDA PVTVSSNVDL AVFKERLRML
TVGGFYGLHE SDLDKVFHLP TTTFIGGKES ALPLREIIRR LEMAYCQHIG VEFMFINDLE
QCQWIRQKFE TPGIMQFTNE EKRTLLARLV RSTRFEEFLQ RKWSSEKRFG LEGCEVLIPA
LKTIIDKSSE NGVDYVIMGM PHRGRLNVLA NVIRKELEQI FCQFDSKLEA ADEGSGDVKY
HLGMYHRRIN RVTDRNITLS LVANPSHLEA ADPVVMGKTK AEQFYCGDTE GKKVMSILLH
GDAAFAGQGI VYETFHLSDL PSYTTHGTVH VVVNNQIGFT TDPRMARSSP YPTDVARVVN
APIFHVNSDD PEAVMYVCNV AAEWRSTFHK DVVVDLVCYR RNGHNEMDEP MFTQPLMYKQ
IRKQKPVLQK YAELLVSQGV VNQPEYEEEI SKYDKICEEA FARSKDEKIL HIKHWLDSPW
PGFFTLDGQP RSMSCPSTGL TEDILTHIGS VASSVPVENF TIHGGLSRIL KTRGELVKNR
TVDWALAEYM AFGSLLKEGI HIRLSGQDVE RGTFSHRHHV LHDQNVDKRT CIPMNHLWPN
QAPYTVCNSS LSEYGVLGFE LGFAMASPNA LVLWEAQFGD FHNTAQCIID QFICPGQAKW
VRQNGIVLLL PHGMEGMGPE HSSARPERFL QMCNDDPDVL PDLEEANFDI NQLYDCNWVV
VNCSTPGNFF HVLRRQILLP FRKPLIIFTP KSLLRHPEAR TSFDEMLPGT HFQRVIPENG
PASQNPEKVK RLLFCTGKVY YDLTRERAAR NMAEEVAITR IEQLSPFPFD LLLKEVQKYP
NAELAWCQEE HKNQGYYDYV KPRLRTTINR SRPVWYAGRD PAAAPATGNK KTHLTELQRL
LDTAFNLDAF KNLA
//
