ID A0A2K5H9H6_COLAP Unreviewed; 365 AA. AC A0A2K5H9H6; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 27-MAR-2024, entry version 25. DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280}; DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280}; DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Colobinae; Colobus. OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000000983.1, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000000983.1} 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: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00006936}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A2K5H9H6; -. DR Ensembl; ENSCANT00000003996.1; ENSCANP00000000983.1; ENSCANG00000002412.1. DR Proteomes; UP000233080; Unplaced. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt. 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 Gene3D; 3.40.50.970; -; 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; IPR029061; THDP-binding. 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 SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1. PE 3: Inferred from homology; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000233080}; KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT DOMAIN 48..86 FT /note="2-oxoglutarate dehydrogenase E1 component N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF16078" FT DOMAIN 257..345 FT /note="Dehydrogenase E1 component" FT /evidence="ECO:0000259|Pfam:PF00676" SQ SEQUENCE 365 AA; 40941 MW; 90ECF5A236CA7713 CRC64; MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN GVDYVIMGMP HRYGRLNVLA NVIRKELEQI FCQFDSKLEA VCGAQACPTH PAWAQTAPGP HRVCA //