ID   A0A3Q2DXR5_CYPVA        Unreviewed;       875 AA.
AC   A0A3Q2DXR5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=2-oxoadipate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040865};
DE   AltName: Full=2-oxoadipate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041619};
DE   AltName: Full=Alpha-ketoadipate dehydrogenase {ECO:0000256|ARBA:ARBA00042817};
DE   AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042094};
DE   AltName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial {ECO:0000256|ARBA:ARBA00042537};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024683.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000024683.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoadipate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-glutaryldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:69576, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:17726, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57499, ChEBI:CHEBI:83099, ChEBI:CHEBI:184385;
CC         Evidence={ECO:0000256|ARBA:ARBA00043772};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC         Evidence={ECO:0000256|ARBA:ARBA00043772};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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; A0A3Q2DXR5; -.
DR   Ensembl; ENSCVAT00000003566.1; ENSCVAP00000024683.1; ENSCVAG00000009032.1.
DR   GeneTree; ENSGT00950000183125; -.
DR   Proteomes; UP000265020; Unplaced.
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; 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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          574..777
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   875 AA;  97619 MW;  40ECFE469B306FA5 CRC64;
     MSAVLFLKTC MRRLPPNAAG QVLGCCYHTE RGVYGYRPKQ LGVENTSQRE RIAALNQDHG
     LARLVEAYRT HGHKAAKINP LLPQQPVVDS VPEIEMLAAA VRGTLNTSGL RHFGKAQASV
     EEVQTYLEQV YCGHLSVETS QLSSLEEREW FADRFEELKR ESFSPEEKKL LAKLMLESQE
     FDHFLATKFA TVKRYGGEGA ESMMGFFYEL FHQSAHKGVT DIVIGMPHRG RLNLLTGLLK
     FPPELMFRKM RGLSEFPDTS PAIGDVLSHL TSSVELDLGA GHPLHVTMLP NPSHLEAINP
     VAQGKTRARQ QLRKEGDYSP EENAYPGDQV ICLQVHGDGS FTGQGIVPET LTLSNLPHYR
     VGGSIHLIVN NQVGYTTPSD RGRSSLYCSD VGKMVNCAVI HVNGDDAEDV LRAARLAVDY
     QRQFRKDIIL DLICYRQWGH NELDEPFFTN PAMYKIIRSR QSAPDSYSDQ LISEGLMTEA
     ERAEIKSSYY SMLNEKLSGM TLYSPPPTNL QGRWGDLVEP RARVTTWDTG VPAQLLQFIG
     AKSVDIPEQI SLHNHLLKTH VQARLQKLEE GTKLDWSTAE ALAFGSLLCQ GFNIRISGQD
     VGRGTFSQRH AMVVCQETND TYVPLNHISP QQTGFLEVCN SPLSEEAVLG FEYGMSIAQP
     KLLPIWEAQF GDFFNGAQII FDTFISGGEA KWLLQCGMVI LLPHGYDGAG PEHSSCRMER
     FLQMCDSKEE GVDGDNVNMA VVNPTTPTQY FHLLRRQMIR NFRKPLIVVG PKTLLRFSGA
     VSSLSELGPG TSFRPVLGDP SVPAEGVQKV VLCSGKHYYA LLKQREASAA NQNTALIRVE
     ELCPFPLEAL QQELRKYPKA KEPFSWLEHP SSNWK
//