ID B3SFC4_TRIAD Unreviewed; 341 AA.
AC B3SFC4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
DE Flags: Fragment;
GN ORFNames=TRIADDRAFT_34977 {ECO:0000313|EMBL:EDV18571.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV18571.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV18571.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV18571.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(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; DS986137; EDV18571.1; -; Genomic_DNA.
DR RefSeq; XP_002118943.1; XM_002118907.1.
DR AlphaFoldDB; B3SFC4; -.
DR STRING; 10228.B3SFC4; -.
DR EnsemblMetazoa; TriadT34977; TriadP34977; TriadG34977.
DR GeneID; 6760157; -.
DR KEGG; tad:TRIADDRAFT_34977; -.
DR CTD; 6760157; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_2_3_1; -.
DR InParanoid; B3SFC4; -.
DR OMA; ERESTMM; -.
DR OrthoDB; 3597773at2759; -.
DR PhylomeDB; B3SFC4; -.
DR Proteomes; UP000009022; 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; 3.40.50.970; -; 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; IPR029061; THDP-binding.
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 SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 7..43
FT /note="2-oxoglutarate dehydrogenase E1 component N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16078"
FT NON_TER 341
FT /evidence="ECO:0000313|EMBL:EDV18571.1"
SQ SEQUENCE 341 AA; 39361 MW; CD7CD3190BB27836 CRC64;
MSDNSDFFSQ NAIFIEELYN KYLKEPDSVD DIWKKYFADL KENVDDFNNY FSGPSWKKRG
NKIVGYQDKV KKDVKNSKTE SNNQFNDLTV KAIQLIDAFR IYGHIAVKLD PLNLNNSAFP
KELDYKNYGI KDEDLEQKIY LNEIFGQNEM QFKELYQHLL NTYSGRFAIE FSHIDNLQER
EWLRTKIESD AGVINLSKDK KFKILDSIAK VEMFQEYLHT KFPGAKRFSI EGGEGTITAL
EEIIQTSAQD NFKEIVFGMA HRGRLSILTK VINKPYYAVF SEFKGGIFVP DDINLPGDVK
YHLAFSSDIE IDGRSIHLTL TPNPSHLETV NSVVLGRVRA K
//
