ID   B8CBX3_THAPS            Unreviewed;      1015 AA.
AC   B8CBX3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=THAPSDRAFT_269718 {ECO:0000313|EMBL:EED89203.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|EMBL:EED89203.1, ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED89203.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED89203.1};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED89203.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED89203.1};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
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}.
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DR   EMBL; CM000648; EED89203.1; -; Genomic_DNA.
DR   RefSeq; XP_002293467.1; XM_002293431.1.
DR   AlphaFoldDB; B8CBX3; -.
DR   STRING; 35128.B8CBX3; -.
DR   PaxDb; 35128-Thaps269718; -.
DR   EnsemblProtists; EED89203; EED89203; THAPSDRAFT_269718.
DR   GeneID; 7450803; -.
DR   KEGG; tps:THAPSDRAFT_269718; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; B8CBX3; -.
DR   OMA; RDSYCRT; -.
DR   Proteomes; UP000001449; Chromosome 13.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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   ECO:0000313|EMBL:EED89203.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          631..857
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1015 AA;  114945 MW;  3A7C94E0152488DB CRC64;
     MRLSHGSGRH SSSNYISHHG NNSSIIRHLS THPSKNDSFL SASSSLYIES MLERYEQDPD
     SVPESWRTYF EMGAADASTS SSGEEAMFNQ PTIVLSTHLI RAYQVNGHRS ANLDPLGLHT
     NESFPSHDGF AATLNVGFHG FDPNKDMDRE LNFKGVHTGG NKGFLEDLTS MPGKVTLRKV
     LDRLRQTYCG TIGVEYMHIG STEQCNWIRE RVEHPSFLQC DREKKIHIYE RLCFADTFEN
     YMAHKFNTTK RFGLDGGEAI VPALKDAIDR ASELGAHSFI IGMPHRGRLN VLANVMRKPM
     TTIFSEFQGT HYEMGYYTKM KEDWGSSGDV KYHLGSSMDR TYPDGRKIHL SLVANPSHLE
     CVNPVVLGKA RAKQFYCGDS DEDMRNVVPI LLHGDAAFAG QGVVYETMQM MGVDDFKVGG
     TLHVIVNNQI GFTTNPINSR STPYASDLGK AFNCPIFHCN GDDPVAVSRA LETAVEWRHE
     WGTDVVIDMI CYRRNGHNEL DQPMFTQPKL YKAITRHPST LEIFEKKLIE EGTMSKEEVE
     EIRAFTLQSY ETDYEASKTY KPKPEDWLSS KWSGFKSPRQ HSRIRPTGVD IDTLRYIGNK
     AGEVPEGFKI HRQMNKIFKA RQTMAQEGTE IDWGLAEAMA FGSLLLEGNH VRLTGQDVQR
     GTFSHRHAVV KDQDTEEEYT PLNSLARILS MSAPLEELRL PDTQAKLTVR NSILSEFAVL
     GFEHGYSLEN PNALVLWEAQ FGDFVNGAQV MLDQFIAAGE DKWLRQSGLV MLLPHGYDGQ
     GAEHSSCRVE RYLQMVEEDP HHIPPMGKDE RNQIQKVNWQ IVNCTTPANY FHCLRRQIHR
     DFRKPLIVVA PKNLLRNKRC VSSLDDMGPG TIFHRTFDET DEVIKNNPEN VKTLVFCTGQ
     IYYELVGERE KLGRHDVAIV RLEQIAPFAF DKVALYCSKY GNAEVIWAQQ EPKNMGAYSY
     VLPRLMTATR EINNNEKRAR YVGRLVSSAP ATGMSKIHLK EYRDIMEGVF GEASE
//