ID   A0A3B4YWM3_SERLL        Unreviewed;      1016 AA.
AC   A0A3B4YWM3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=OGDHL {ECO:0000313|Ensembl:ENSSLDP00000027154.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000027154.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000027154.1}
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   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   AlphaFoldDB; A0A3B4YWM3; -.
DR   STRING; 1841481.ENSSLDP00000027154; -.
DR   Ensembl; ENSSLDT00000027989.1; ENSSLDP00000027154.1; ENSSLDG00000021061.1.
DR   GeneTree; ENSGT00950000183125; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000261360; 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; 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:SF5; 2-OXOGLUTARATE DEHYDROGENASE-LIKE, MITOCHONDRIAL; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          644..857
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1016 AA;  115084 MW;  D75724A0A7AE648E CRC64;
     MSQFRALAGV LRGGCAGGSQ WLRGRGGGPA RRWVDLRRGC SSGAAPVPSA VASSSSYVEE
     MYFAWLEDHK NVHESWDAFF RNIQASSPSG EAGERRPSAL LQGRVLSHSP DMTQKVVEDH
     LAVHTLIRAY QIRGHHVAQL DPLGILEADL DSFVPSDLIT TIDKLGFYGL DESDLDRSFQ
     LPPTTFIGGE NTTLPLREII RRLETSYCGH IGVEFMFINN VDQCQWIRQK FETPGIMQFT
     NAEKRTLLAR LIRSTRFEDF LARKWSSEKR FGLEGCEVLI PALKTIIDKS SAAGIDSVIM
     GMPHRGRLNV LANVIRKDLD QIFCQFDPKL EAADEGSGDV KYHLGMYHER INRETDKDIT
     LSLMANPSHL EAVDPVVMGK AKAEQFYRGD TQGKKVMSIL MHGDAAFAGQ GVVYETFHLS
     ELPSYTTHGT IHVVVNNQIG FTTDPRVARS SPYPTDVARV VNAPIFHVNA DDPEAVMYVC
     QVAAEWRNTF NKDVVIDLVS YRRFGHNEMD EPMFTQPLMY KQIRRQEHVL KKYSDKLISE
     GVVTLQEFEE EVAKYDKICE EAYTSSKDEK ILHIRHWLDS PWPDFFTAEG EPRSMSCVPS
     GLEEEVLQHI GHTASSVPLE DFKIHPGVSR ILRVRADLVK NRQMDWALGE YMAFGSLLKD
     GIHVRLSGQD VERGTFSHRH HVLHDQEVDK RICVPMNHLW ANQAPYTVCN SSLSEYGVLG
     FELGFAMASP NALILWEAQF GDFHNTAQCI IDQFISSGQA KWVRNNGIIL LLPHGMEGMG
     PEHSSARPER FLQMSNDDPD HFPEFNGDFE VQQLHDCNWI VVNCSTPANY CHVLRRQILL
     PFRKPLIIFT PKSLLRHPDA RSSFDDLAKG TKFKRLIPDQ GPASQNPGQV KRVIFCTGKV
     YYELAKERKQ QTLEKDVAII RLEQIAPFPF DLVRAEAEKY ANAELVWCQE EHKNMGYYDY
     VRPRFLTVMA NRKPIWYVGR DPAAAPATGN KSTHLNELRR FMDTVFNLSA FQGKDL
//