ID A0A3Q2FP96_CYPVA Unreviewed; 872 AA.
AC A0A3Q2FP96;
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:ENSCVAP00000007295.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000007295.1}
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}.
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DR RefSeq; XP_015246515.1; XM_015391029.1.
DR AlphaFoldDB; A0A3Q2FP96; -.
DR Ensembl; ENSCVAT00000003550.1; ENSCVAP00000007295.1; ENSCVAG00000009032.1.
DR GeneID; 107095058; -.
DR CTD; 55526; -.
DR GeneTree; ENSGT00950000183125; -.
DR OrthoDB; 3597773at2759; -.
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 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 523..726
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 872 AA; 97354 MW; 221825720C4DA6F6 CRC64;
MSAVLFLKTC MRRLPPNAAG QVLGCCYHTE RGVYGYRPKQ LGVENTSQRE RIAALNQGLR
HFGKAQASVE EVQTYLEQVY CGHLSVETSQ LSSLEEREWF ADRFEELKRE SFSPEEKKLL
AKLMLESQEF DHFLATKFAT VKRYGGEGAE SMMGFFYELF HQSAHKGVTD IVIGMPHRGR
LNLLTGLLKF PPELMFRKMR GLSEFPDTSP AIGDVLSHLT SSVELDLGAG HPLHVTMLPN
PSHLEAINPV AQGKTRARQQ LRKEGDYSPE ENAYPGDQVI CLQVHGDGSF TGQGIVPETL
TLSNLPHYRV GGSIHLIVNN QVGYTTPSDR GRSSLYCSDV GKMVNCAVIH VNGDDAEDVL
RAARLAVDYQ RQFRKDIILD LICYRQWGHN ELDEPFFTNP AMYKIIRSRQ SAPDSYSDQL
ISEGLMTEAE RAEIKSSYYS MLNEKLSGMT LYSPPPTNLQ GRWGDLVEPR ARVTTWDTGV
PAQLLQFIGA KSVDIPEQIS LHNHLLKTHV QARLQKLEEG TKLDWSTAEA LAFGSLLCQG
FNIRISGQDV GRGTFSQRHA MVVCQETNDT YVPLNHISPQ QTGFLEVCNS PLSEEAVLGF
EYGMSIAQPK LLPIWEAQFG DFFNGAQIIF DTFISGGEAK WLLQCGMVIL LPHGYDGAGP
EHSSCRMERF LQMCDSKEEG VDGDNVNMAV VNPTTPTQYF HLLRRQMIRN FRKPLIVVGP
KTLLRFSGAV SSLSELGPGT SFRPVLGDPS VPAEGVQKVV LCSGKHYYAL LKQREASAAN
QNTALIRVEE LCPFPLEALQ QELRKYPKAK DFIWSQEEPE NMGPWSFVAP RFEKQLACKL
RLVSRPALPA PAVGIGTLHH QQQEAILTAT FS
//
