ID A0A1Q9DLF8_SYMMI Unreviewed; 547 AA.
AC A0A1Q9DLF8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000313|EMBL:OLP95979.1};
GN Name=ogdh {ECO:0000313|EMBL:OLP95979.1};
GN ORFNames=AK812_SmicGene21859 {ECO:0000313|EMBL:OLP95979.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP95979.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP95979.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP95979.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OLP95979.1}.
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DR EMBL; LSRX01000484; OLP95979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9DLF8; -.
DR OMA; YMHINDP; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000186817; 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 InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; 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; PF00676; E1_dh; 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:UP000186817};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 98..424
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 547 AA; 61077 MW; B8CADDB7B728244C CRC64;
MGKHPSQKHA DGFHGFTAAD MEKKFQVSLV GLSAEHTLKE ILATLQSTYS GSVGIEYMHI
GDLQKIDWIR QRVEDPNFIP SDKNKLLKVY KELLKVDTFE MFLNTQYKTT KRFGVDGGEA
AVAGVNAAIE KAATLGMSEC VIGMPHRGRL NVLTNVVRKP LVQMFAEFKG THYDFEKLVE
KSDEDDWLFA GDVKYHLGTS QVFSFEGGKT ITATLEANPS HLETVNTVTL GRARAKQYYL
GNTEESRTRV LPILFHGDAS FAGQGVVYET MQLAHVQEFD VGGTIHVIIN NQVGFTTDPV
DDRSTLYTSD LGKSFNLPIL HVNGDDPVAV TSAFELAAEW RQTWQTDVIV DVVCYRRFGH
NETDAPEYTQ PVLYKQINKH PRTEAVYANS LVDSGAATPQ ELEAMKSSIW KEHEAAFKEA
DSFKPSEEAE WVATKWEGFV RPTDMSNSHP TGVDVELLRK IGERLCYTPD GFKVHNGLKR
QLKKKMEDLE GGETIDWATA EALAFGSLLL EGNHVRMKGL CETGPIVKES KSEPLVDVCP
RCFRSSR
//
