ID A0A096LUK7_POEFO Unreviewed; 1029 AA.
AC A0A096LUK7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ENSPFOP00000022848.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000022848.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000022848.1}
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 EMBL; AYCK01014432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096LUK7; -.
DR STRING; 48698.ENSPFOP00000022848; -.
DR Ensembl; ENSPFOT00000024386.1; ENSPFOP00000022848.1; ENSPFOG00000018716.2.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR OMA; CEDAFAH; -.
DR Proteomes; UP000028760; 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:0060047; P:heart contraction; 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:UP000028760};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 658..871
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1029 AA; 115890 MW; B0617E485C71563F CRC64;
MHHLRTTVAR LGPLAAAQTA QIAPQSRLLA LERGTRTFQP VRSLRASVAA EPFLNGTSSN
YVEEMYYAWL EDPRNVHKSW DIFFRNANAG APPGAAYQSP PPLSGPSDGT MGVRALVGAQ
PNVEKLVKDH LAVQSLIRAY QVRGHHIAKL DPLGISCVDF DDAPCTVGFQ NVVTLSVKYS
LYGLTEGDLD KVFRLPASTF IGGNDSALPL REIIRRLEMA YCQHIGVEFM FINDLEQCQW
IRQKFETPGI MQFSLEEKRT LLGRMIRSTR FEEFLQRKWS SEKRFGLEGC ESLIPALKTI
IDRSSQCGVE SMILGMPHRG RLNVLANVIR KDLDQIFCQF DSKLEAADEG SGDVKYHLGM
YHRRMNRVSD RYITLSLVAN PSHLEAVDPV VQGKTKAEQF YSGDTEGKRV MSILLHGDAA
FAGQGIVYET FHLSDLPSYT THGTIHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF
HVNADNPEAV MFVCNVAAEW RNTFHKDVVV DLVSYRRNGH NEMDEPMFTQ PLMYKQIKKQ
KGVLQKFVEK LVAEGVITTQ HYEEEVARYD KICEDAFAHS KDEKILHIKH WLDSPWPGFF
TLDGQPKTMS CPSTGIREDE LCHIGNVAAS VPLEDFMIHG GLSRILKGRA HMVSKRVCDW
ALGEYMAFGS LLKEGIHVRL SGQDVERGTF SHRHHVLHDQ NVDKRICIPM NSISPDQAPY
TVCNSSLSEY GVLGFELGFA MASPNALVLW EAQFGDFHNT AQCIIDQFIS SGQAKWVRQN
GIVLLLPHGM EGMGPEHSSA RPERFLQMCN DDSDVFPKVT GDFAVHQLYD CNWIVVNCST
PANYFHVLRR QILLPFRKPL IVFTPKSLLR HPEAKSSFDD MLPGTHFQRL IPDEGPAAVG
PQNVKRVVFC TGKIYYDLIR ERKSRGLEDA VAVVRIEQLS PFPFDLVKAE ADQYQNADLV
WCQEEHKNQG YYDYVKPRLR TTLNRTRPIW YAGREPAAAP ATGNKHTHLT ELQHLLDAAF
DLETSPGKL
//
