ID   D8S4X1_SELML            Unreviewed;       969 AA.
AC   D8S4X1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=SELMODRAFT_152569 {ECO:0000313|EMBL:EFJ20348.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ20348.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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; GL377602; EFJ20348.1; -; Genomic_DNA.
DR   RefSeq; XP_002978362.1; XM_002978316.1.
DR   AlphaFoldDB; D8S4X1; -.
DR   STRING; 88036.D8S4X1; -.
DR   EnsemblPlants; EFJ20348; EFJ20348; SELMODRAFT_152569.
DR   GeneID; 9653666; -.
DR   Gramene; EFJ20348; EFJ20348; SELMODRAFT_152569.
DR   KEGG; smo:SELMODRAFT_152569; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; D8S4X1; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          588..801
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   969 AA;  109484 MW;  0C4D6FE589684BF4 CRC64;
     MQTAAASAPR SVPLSRLTDN FLDGTSSVYL EELQRAWEAD PKSVDESWDN FFQNFTGKAA
     SSPGVSGQTI QESMRLLLLV RAYQVNGHMK AKLDPLGLDE RVPPEDLNPA LYGFTEADLD
     REFFIGVWRM SGFLSENRPV QTLRAILKRL EQAYCGTIGY EYMHISDREK CNWLREKIEQ
     HVPSKYSKER QITILDRLIW GTKFENFLAQ KWTAKRFGLE GCETLIPGMK EQIDRAADLG
     VESVVIGMPH RGRLNVLGNV VRKPLRQIFS EFAGGTKPAE SGYSGSGDVK YHLGTSYDRP
     TRTGKHIHLS LVANPSHLEA VDPVVVGKTR AKQYYSDDYE RKKNMAILLH GDGSFSGQGV
     VYETLHLSDL PNYTTGGTIH IVVNNQVAFT TDPRSSRSSP YCTDVAKALN APIFHVNGDD
     VEAVVHACEL AAEWRCQFKA DVVVDIVCYR RFGHNEIDEP SFTQPKMYQV IKNHPTSLEL
     YEKKLIESGQ ISEETVKKIH DKVYGILSEE FESSKDYVPK TQDWLAAYWS GFKSPEQLSR
     LRNTGVKPEV LKNVGKKITT LPPSFTAHRA IKRVYEQRAQ MIETGDGVDW ATAEALAFAT
     LLAEGNHVRL SGQDVERGTF SHRHAVVHDQ ETGERYCPLD HVVTNQKEEM FTVSNSSLSE
     FGVLGFELGY SMENPNSLVC WEAQFGDFSN GAQVIFDQFL SSGEAKWLRQ TGLVCMLPHG
     YDGQGPEHSS ARLERFLQMS DDHPFVIPEM EVSLRKQIQE CNWQVVNVTT PANYFHVLRR
     QLHRDFRKPL IIMSPKNLLR HSSCRSNLSE FDDVQGHPGF DKQGTRFKRL IKDKNDHGTV
     EPEIRRLVLC SGKVYYELDE ERERVGAKDV AICRVEQLCP VPYDLLQREL KRYPNADVVW
     CQEEPMNMGA FSYIAPRLGT AMLSVNRGSF GDIKYVGRPP SAATATGFAA VHKMEQTELV
     QKALQAQKM
//