ID   A0A078B5M2_STYLE        Unreviewed;       939 AA.
AC   A0A078B5M2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Oxoglutarate dehydrogenase {ECO:0000313|EMBL:CDW88818.1};
GN   Name=Contig5274.g5652 {ECO:0000313|EMBL:CDW88818.1};
GN   ORFNames=STYLEM_17943 {ECO:0000313|EMBL:CDW88818.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW88818.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW88818.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW88818.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CCKQ01016924; CDW88818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078B5M2; -.
DR   EnsemblProtists; CDW88818; CDW88818; STYLEM_17943.
DR   InParanoid; A0A078B5M2; -.
DR   OMA; TPAQYYH; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000039865; 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   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; 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:UP000039865};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          565..780
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   939 AA;  108092 MW;  9BC1B32A9FE2AFB3 CRC64;
     MLLRNLIKQQ KTNQSQILMN LMGKQFSRQV KIPKSHNLLG YIEHYQKHGH TQSKLDPLGL
     KNPDRCDTFE TDHWQLNPLE NIQTYPLDYR VSTHLQDKVA TISDLHEYLN NVYAGSVGIE
     FDHVHNQEER LWLYENHEKV MHESISSQEK FKILQLLTRT EEMEKFLQKR FATHKRYSSE
     GSEAISVAIN AIIAEASHVE KGEMEYAVLG MPHRGRLATL IVANDFPMRN LIYKVKGNNE
     IPEEINDRID DMPTHIAVSN TKKFSHGADN SKNRDVTLTM IHNPSHLESQ NSISMGKTRA
     KQDDFGNLKK VLNIQGHGDA AFTGQGAAYE ALTLCKLPKF QCNGTIHFIT NNQVGFTTDN
     ADGRSFPHAS DIVKPFGIPI IRVNAHDVEA VSRVCKLAAR YWHQYGKDIL IDMIGYRKYG
     HNEVDEPSFT QPKMYEKIRD MKSLPHQYAE KLVQEGVIKE QAYQKMIDQI SNHYEEEFKE
     AEKFKPTLET TKDPNYKGSR SLTHKWKDMD FSQNGKEPQH SGYEKDKLIR IAKSSVELPP
     NIQPHSRLQR MHIANRLKSI EENKFDWATA EAMAYGSLLI DGYNVRLTGE DVERGTFSQR
     HAVFHCQQEH GEYTTPLKES QFMQSHSKGR FQVYNSNLNE LGVMGYEYGY SLESPKNLVQ
     WEAQFGDFYN PAQLIVDQYL MCSEAKWLRQ SGLILLLPHG FDGSGPEHST CHIERFLQNI
     NSQAYDNLNG PYDNLTAQNI NFQFAQMTMP SNYFHLLRRQ MLRNYRKPMV IAAPKIGLKH
     PKAVSGIDEF LPGTRFQPTI VNKFGQGDVK KVIFCSGKVY FDIAQKLETD AAQLKNTFAV
     IRVEELAPFP INEIQTHLQS LGVKSSAEYV WVQEECLNEG AFQFAKLHID RALRKLQFKQ
     SEMYYVGRPS QHSFATGSPA DYKKESQQLW KDFESRIYN
//