ID   A0A383ZUN5_BALAS        Unreviewed;      1010 AA.
AC   A0A383ZUN5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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|RefSeq:XP_007178776.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007178776.1};
RN   [1] {ECO:0000313|RefSeq:XP_007178776.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007178776.1};
RG   RefSeq;
RL   Submitted (JAN-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   RefSeq; XP_007178776.1; XM_007178714.1.
DR   AlphaFoldDB; A0A383ZUN5; -.
DR   CTD; 55753; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000261681; 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   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          638..851
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1010 AA;  114557 MW;  C611318AD61FB2A1 CRC64;
     MSQLRLLPSR LGAQASRLLA THGVHRFSWY SRSSGPPATF PSSKVGGGSS YMEEMYFAWL
     ENPQSVHKSW DSFFRKASEE ASYGPAQPRP LSVVPESRPA VLSRTKTSKL VEDHLAVQSL
     IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLREADLD KEFQLPTTTF
     IGGSENTLSL REIIRRLENT YCQHIGLEFM FINDVEQCQW IRQKFETPGV MQFSSEEKRT
     LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGIE NVILGMPHRG
     RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNITLSLVAN
     PSHLEAVDPV VQGKTKAEQF YRGDAQGKKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
     TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
     RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHRQ VPVLKKYADK LIAEGAVTLQ
     EFEEEIAKYD RICEEAFGRS KDKKILHIKH WLDSPWPGFF TVDGEPKSMT CPATGIPEDM
     LTHIGEVASS VPLEDFKIHT GLSRILRGRA DMTRKRTVDW ALAEYMAFGS LLKEGIHVRL
     SGQDVERGTF SHRHHVLHDQ EVDRRTCVPM NHLWPDQAPY TVCNSSLSEY GVLGFELGYA
     MASPNALVLW EAQFGDFHNT AQCIIDQFIS TGQAKWVRHN GVVLLLPHGM EGMGPEHSSA
     RPERFLQMSN DDSDAYPAFT QDFEVRQLYD CNWIVVNCST PASYFHVLRR QILLPFRKPL
     IIFTPKSLLR HPEAKSSFDQ MVSGTSFQRV IPEDGAAAQA PGQVRRLIFC TGKVYYDLVK
     ERSSQGLDQH VAITRLEQIS PFPFDLIKRE AEKYPGAELV WCQEEHKNMG YYDYISPRFM
     TILGRARPIW YVGRDPAAAP ATGNRNTHLV SLKKFLDTAF NLQAFEGKTF
//