ID A0A1R2AYE2_9CILI Unreviewed; 962 AA.
AC A0A1R2AYE2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN ORFNames=SteCoe_32714 {ECO:0000313|EMBL:OMJ69539.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ69539.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ69539.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ69539.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMJ69539.1}.
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DR EMBL; MPUH01001186; OMJ69539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2AYE2; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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:UP000187209};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 599..812
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 962 AA; 109341 MW; 406551DAB51A62D8 CRC64;
MWRGVTKLCK FPTRCYSDNF YSTTNALYIE QLHERWLSNP SSIHPSWQAF FSATDAGQSQ
AFIAPDFTKL ELGEKDGTSS YVSDVLKVQL LLQGFQRYGC LIADLDPLKL TEHVISNQAE
VRIPGIIRME NYKFTEQDMD REFDIGSDLI TGFMKTDGPH RGKWKLRDLI ERCREVYTGK
IGFEFMHIPF RDECNWIKER IESDELFSNS KERKIEIFTK VAQAELLEDF FHKKFSTHKR
FGMDGSETAV LALHSLIDRA IENGVDNFVI GMPHRGRLNV MANILETSLE EMFGLFYGIG
YRQVEEGDVK YHLGQTMVKE IKGRTVTIRL LANPSHLEAV DPVVVGTARA IQNKQLNRSR
TMAIVLHGDA ALAGQGVVYE TMQMEDLFDY STGGVVHMVI NNQIGFTTTP REARSGQFPT
EIAKAIGAPI FHVNGDCPEE VDFVSRLAAD WRSEFRGGVF IDIIGYRRYG HNELDEPLFT
NPKMYQLIQK HTSILQKYTK ELIDQKILDE DSVNSIKRSI IDGYEKMFAM VKLKSETKTE
IKTHEREGIS DVFRTGIEVP KLQELGVKLH SLPKDLKPHP QITKIYQNRL NTIEKGSGID
WATAEALAWA TIMSEEKMDV RISGQDVQRG TFSHRHSVIH DQVVDRKKYI PLNHLSLNQG
SFTAANSHLS EYAVLGFEHG YTLANPNSLV MWEAQFGDFV NGAQIIIDQF ITSAEAKWGQ
ESGLVLLLPH GYDGQGAEHS CARLGRFLQA SSEDPYTIPD QIIKEYKQCF FNNIQVANPT
TPANYFHFLR RQIKREFRKP LIVMSPKRLL RHKSAVSDLA ELADDRVKRV YDDANFDGSN
VSEVRKVILC SGQVYYDLIE ERKKRGINNI AICRIEQLAP FPFEKVQEIG KKYSKAEFQW
VQEEPLNLGA WQYVETRINT SLGGQGKHDV SVVSRPASAA AATGYLSVHN AELVALLDKS
MN
//
