ID   A0A3Q1I7U1_ANATE        Unreviewed;      1014 AA.
AC   A0A3Q1I7U1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 23.
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};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000000636.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000000636.2}
RP   IDENTIFICATION.
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; A0A3Q1I7U1; -.
DR   Ensembl; ENSATET00000000649.2; ENSATEP00000000636.2; ENSATEG00000000473.2.
DR   GeneTree; ENSGT00950000183125; -.
DR   Proteomes; UP000265040; Unplaced.
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:UP000265040};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          641..854
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1014 AA;  114901 MW;  7ED8E46CBF0D8757 CRC64;
     MHCLRTTVAK LRPLTAAQSL SQNRLAERGL RMFQPKRHLN SSVAAEPFLN GTSSNYVEEM
     YYAWLENPRN VHKSWDIFFR NANAGALPGA AYQSPPSLSG TRVQALVGAQ PNVEKLVEDH
     LAVQSLIRAY QVRGHHIAKL DPLDISCVDF DDAPCAVGFQ NVGFYGLTQS DLDKVFRLPT
     TTFIGGKESA LPLREIIRRL EMAYCQHIGV EFMFINDVEQ CQWIRQKFET PEVMKFNLEE
     KRTLLARMIR STRFEEFLQR KWSSEKRFGL EGCESLIPAL KTIIDKSSQS GVESVILGMP
     HRGRLNVLAN VIRKDLDQIF CQFDSKLEAA DEGSGDVKYH LGMYHKRMNR VSDREIMMSL
     MANPSHLEAV DPVVQGKTKA EQFYCGDTQG KRVMSILLHG DAAFAGQGIV YETFHLSDLP
     SYTTHGTIHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNADDP EAVMYVCSVA
     AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKKI KKQKGVLQTF SEKLIAEGVV
     TTQEYEEEVA KYDKICEEAY TRSKDEKILH IKHWLDSPWP GFFTQEGHPK SMSCPPTGIS
     EDELGHIGNI AASVPLEDFT IHGGLSRILK GRANMVSQRL CDWALGEYMA FGSLLKEGIH
     VRLSGQDVER GTFSHRHHVL HDQNVDKRIC IPMNYISPDQ APYTVCNSSL SEYGVLGFEL
     GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FISSGQAKWV RHNGIVLLLP HGMEGMGPEH
     SSARPERFLQ MCNDDPDVFP KLSEDFAVQQ LYDCNWIVVN CSTPANYFHV LRRQILLPFR
     KPLIVFTPKS LLRHPEAKSS FDDMLPGTDF KRIIPDDGPA AIRPEKVKRV IFCTGKIFYE
     LTRERKNRGM DDDVAVLRIE QLSPFPFDLV KAEAERYPNA DLVWCQEEHK NQGYYDYVKP
     RIRTTINRTR PVWYAGRGPA AAPATGNKQT HLTELQRLLD TALDLEAFSG KLSS
//