ID   T2ME63_HYDVU            Unreviewed;      1018 AA.
AC   T2ME63;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
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   Name=OGDH {ECO:0000313|EMBL:CDG70394.1};
GN   Synonyms=LOC100203774 {ECO:0000313|RefSeq:XP_012556386.1};
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG70394.1};
RN   [1] {ECO:0000313|EMBL:CDG70394.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole animals {ECO:0000313|EMBL:CDG70394.1};
RX   PubMed=24065732; DOI=10.1093/gbe/evt142;
RA   Wenger Y., Galliot B.;
RT   "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT   bilaterian, euteleostome, and hominidae ancestors.";
RL   Genome Biol. Evol. 5:1949-1968(2013).
RN   [2] {ECO:0000313|RefSeq:XP_012556386.1}
RP   IDENTIFICATION.
RC   STRAIN=105 {ECO:0000313|RefSeq:XP_012556386.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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; HAAD01004162; CDG70394.1; -; mRNA.
DR   RefSeq; XP_012556386.1; XM_012700932.1.
DR   EnsemblMetazoa; XM_012700932.1; XP_012556386.1; LOC100203774.
DR   EnsemblMetazoa; XM_047289575.1; XP_047145531.1; LOC100203774.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000694840; Unplaced.
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   2: Evidence at transcript level;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694840};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          647..861
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          968..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1018 AA;  115575 MW;  8E68DE63E84E9ABB CRC64;
     MYAVRCKLPG IIKGYFLKPV STSNLRKSLP CTSPTVRFYA SSVSAEPFIN GTSGSYVEEM
     YESWQADPKS VHKSWDVFFR NAQKGALPGQ AYQSPPEIYG HPVRYVTEVT MQQTPGNAPS
     SEQVQNLIQD HLAVYSLIRS YQIRGHNLAN LDPLGILHAD LDSKVPEELV LENSGLSQQD
     LDKEFQLPKT TFIGHSGQTM KLRDIIASLE NVYCKSIGLE FMFLTSQNKN TWIRKHFETP
     GVMSLTPEEK RRLLARLVRS TEFENFLAKK WSSEKRFGLE GCEVLIPALK HIIDISNDKG
     VESVIMGMPH RGRLNVLANV CRKPLEQIFT QFNPTLEQQD EGSGDVKYHL GMTHERLNRT
     TNKIIKLSVC ANPSHLEAVD PVVQGKTRAE QFYRGSSDGK QVMSILLHGD AAFAGQGVVY
     ETMHLSDLPN YTTHGTIHVV VNNQIGFTTD PRMSRSSPYC TDVAKVVQCP IFHVNADDPE
     AVMHVCKVAA EYRAEFHKDV VIDLVCYRKN GHNESDNPDF TQPLMYQKIR QQEPCVLKYA
     RKLISENVVT EEEFQSETLK YGLILEETFE TAKQRPQMKI ADWLDSKWGG FFKPHNLLGE
     LQSTGTSLET LTEIGSKFST PPADFNIHPG LKRVLKSRAE MLEEGIVDWA IGEALAIGSL
     LKEKIHVRLS GQDVERGTFS HRHHVLHDQK IDKKTINVLD TISNDYAKYI CCNSSLSEYA
     VLGFELGYSM TNPYSLVMWE AQFGDFMNTA QCIIDQFISS GQDKWVRQSG LVMLLPHGME
     GMGPEHSSAR LERFLQMTKE DPDTFPDYPE ENFELCQNYH TNWFICNITT PANLFHVLRR
     QVYLSFRKPL VIMTPKSLLR LEAARSNLSE MVEGTFFKRL IPEDGPCVKN PKDVKKLIFC
     SGKIYYELIK ERKHRGLDND IAITRIEQLS PFPFDLVRKE CAKYQNASLQ WVQEEHKNHG
     AWQHMQPRIE TSTGNSRRAR YAGRSTASAP ATGNKKQHMV EQQFVVDSAL SLNNLKVN
//