ID A0A059LP93_9CHLO Unreviewed; 984 AA.
AC A0A059LP93;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=H632_c354p0 {ECO:0000313|EMBL:KDD76103.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD76103.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD76103.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD76103.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
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}.
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:KDD76103.1}.
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DR EMBL; AYPS01000354; KDD76103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LP93; -.
DR STRING; 1291522.A0A059LP93; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000026042; 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 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:UP000026042};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 589..809
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 984 AA; 110011 MW; DCB92A618E3A37CE CRC64;
MDGTSSTYLE QLEQQYRADP STVDRSWAAF FRSMDSGISP EALSESYDAF VKTGAKSPLP
IVAEGQSPQE TMRLAMLVRA HQVEGHRAAQ LDPLGLQQVT PPLTLDPAYY GFEERHMDRE
YSLATWNQSG FMAEDRPRRT LREIVRRLRE TYCGSVGFEY MHIDDHEKCN WIRERIELLE
AEAFSKEKKM LVLDRLTWSE MFESFLANKY TAAKRFGLEG CEALIPGMKA AIDRTADLGT
ETIVIGMPHR GRLNILANVM RKPMEQVFSE FAGRRPAGAS ADDYTGSGDV KYHLGTSYDR
PTLSGRQIHL SLMANPSHLE AVNTVALGKV RAKQYYANDE ARRRNLAILL HGDGAFAGQG
IVYETLDMSA LPDYTVGGTI HLVVNNQVAF TTDPKKSRSS PYCTDVAKAL SAPIFHVNSD
DPEAVVRVCE LAAEWRQTWG TDVVIDLVGY RKYGHNEIDE PMFTQPLMYK KIRAMRNVQQ
LYVDRLLREG SVTSEEVKGV TDKVEKLLHD SFENAKAYKP KTSDWLSSYW KGFRSPHQLS
RIRNTGVPAN ALRDVGQIIT TLPPGVTPHR QIGKVYEARR AALESGEGVD WAFAEALAFG
TLLREGNHVR LSGQDVERGT FSHRHAVVHD QTTGERYTPL AAVAEGGHKS QFTVSNSSLS
EFGVLGFELG YSLENPNSLV LWEAQFGDFA NGAQIIFDQF LSSGEAKWLR QSGLTVLLPH
GYDGQGPEHS SARIERYLQM VDDHPYAFPS IDEAQWATGS HMGTRTQNTN MQVCNVSTPA
QYFHVLRRQL HRDFRKPLII FSPKNLLRHP LARSPLSEFD DVPEDSGITG ARFKRLIMDE
RAADRSPHPT PAPGVKKLVF CSGKIYYELA TERARQGKQD EVAIVRVEQI APFPHDLALR
ELRRYTALRE NPAASVVYCQ EEPMNMGAYS YIAPRLQTCM EAAGYDVPSK IAYAGRAPSA
STATGFGEVH AQEQAALIKA ALDV
//
