ID   A0A3Q1FD01_9TELE        Unreviewed;       983 AA.
AC   A0A3Q1FD01;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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:ENSAPOP00000014918.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000014918.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000014918.1}
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   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   AlphaFoldDB; A0A3Q1FD01; -.
DR   Ensembl; ENSAPOT00000033017.1; ENSAPOP00000014918.1; ENSAPOG00000017961.1.
DR   GeneTree; ENSGT00950000183125; -.
DR   Proteomes; UP000257200; 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; -; 2.
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   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; 2.
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:UP000257200};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          648..824
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   983 AA;  111031 MW;  81F3D7BD4BAD21CE CRC64;
     MSQFRALAGV LKGGCAGGNQ LLRGCARGPA RRWVDPKRGC SSSSSSRTEP LLPAVASSSS
     YVEEMYFAWL EDHKNVHESW DGFFRNIQAS SPSGEAGVTR PSTLLQGRVL SHSLDVAQKV
     VEDHLAVHTL IRAYQIRGHH VAQLDPLGIL EADLDSFVPS DLITTIDKLG FYGLDESDLD
     RSFQLPSTTF IGGQEATLPL REIIRRLETS YCGHIGVEFM FINNVDQCQW IRQKFESPGI
     MQFTNAEKRT LLARLIRSTR FEDFLARKWS SEKRFGLEGC EVLIPALKTI IDKSSAAGID
     SVIMGMPHRG RLNVLANVIR KDLDQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRETD
     KDITLSLMAN PSHLEAVDPV VQGKAKAEQF YRGDTQGKKV MSILMHGDAA FAGQGVVYET
     FHLSELPSYT THGTIHVVVN NQIGFTTDPR VARSSPYPTD VARVVNAPIF HVNADDPEAV
     TYVCRVAAEW RSTFNKDVVI DLVSYRRFGH NEMDEPMFTQ PLMYKQIRRQ EHVLKKYSDK
     LIAEGVVTLQ EFEEEVAKYD KICEEAYTSS KDEKISHIRH WLDSPWPDFF TAEGEPRSMS
     CLPTGLDEDV LQHIGQTASS VPLEDFKIHP GVSRILRGRA DLVKNRQMDW ALGEYMAFGS
     LLKDGIHVRL SGQDVERGTF SDVELVSFEL GFAMANPNAL ILWEAQFGDF HNTAQCIIDQ
     FISSGQAKWV RNNGIVLLLP HGMEGMGPEH SSARPERFLQ MSKDDPDHIP EFSGDFEVQQ
     LYDCNWIVVN CSTPANYSHV LRRQILLPFR KPLIIFTPKS LLRHPDARSS FDDLAKGTKF
     KRLIPDEGHA SQSPGQVKRV IFCTGKVYYE LAKERKQKNL ESDVAIIRLE QISPFPFDLV
     REEADKYANA ELVWCQEEHK NMGYYDYVRP RFLTVVANKK PIWYVGRDPA AAPATGNKST
     HLNELKRFMD TAFNLSAFQK RDL
//