ID   A0A250WP85_9CHLO        Unreviewed;      1006 AA.
AC   A0A250WP85;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=CEUSTIGMA_g89.t1 {ECO:0000313|EMBL:GAX72633.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX72633.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX72633.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX72633.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
RL   Submitted (AUG-2017) 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:GAX72633.1}.
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DR   EMBL; BEGY01000001; GAX72633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250WP85; -.
DR   STRING; 1157962.A0A250WP85; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000232323; 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; 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:UP000232323};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          610..830
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1006 AA;  112915 MW;  1C745D1521B5E4F5 CRC64;
     MITAILPSIA GLKRAVRPSL LTWTRFLQSS SGINTPAEPK PVAISKLKDS FNDATSVAYL
     EELEKKFNAD PNSIDRTWAS FFTSLDRGVP GEAIAEAYDA FEKGKTSSPM QAAALSTQTI
     QESMKLLMLV RSHQVLGHFA AKLDPLGLDN RKVPAELDPT FYGFKDTDLD REFFIGSWAQ
     AGFLAENRPT RTLREILTRL RETYCGTIGY EYMHIPEPEK CNWIRDKIET VDPLQFSQKE
     KLQILDRVAW SEMFETFLAN KYSSAKRFGL EGGRLNVLAN VVRKPMRQIF SEFSGKPSRA
     NEDEYTGSGD VKYHLGTSYN RPTTNGKMVA LSLLANPSHL EAVNTVVLGK VRAKQYYEDD
     QSRLKSMPIL LHGDGAFSGQ GIVYETLDMS GLIDYTVGGC VHIVVNNQVA FTTDPKDGRS
     SPYCTDVAKS LNAPIFHVNG DDVESVVRVC QLAAEWRQTF KTDVVVDLVC YRKYGHNEID
     EPMFTQPLMY KKIRQHTDPH KLYVQKLLTE GSVSAEQVKE VHEKTLTTLA NEFESSKDYK
     PTKKDWLASH WTGFYSPAQL SRIRNTGVKM DLLKQVGVAI TELPSTFTPH KQIRKVYDNR
     RAMIDTGEGV DWGMAEALAY ATLLSEGNHV RLSGQDVERG TFSHRHAVIS DQSTGEKYIP
     LSNVYPGQKP GQFTVSNSSL SEYGVLGFEL GYSLENPNSL VIWEAQFGDF ANTAQVIFDQ
     FLSSGEAKWL RQTGLTVLLP HGYDGQGPEH SSARMERFLQ MSDENPYELP NVDEAQWFTG
     AHLGTQVQSA NWQLVNCTTP AQIFHVLRRQ IHRQFRKPLV VFSPKNLLRH PKCKSGLYEF
     DDEADDAGIV GVRFKRIIMD DTGLMPKSRA PRPPVEAECK RLVLCTGKVF YDLHARREEL
     GLDKGQLAIV RLEQLAPFPF DLVCRELRRY PNAELVWCQE EPMNMGAYFH VQPRMISCLK
     SEGRSVPDGR LAFAGREPSA STATGFGEVH KKEQADLLNA ALGAST
//