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
//