ID A0A2S7QT82_9HELO Unreviewed; 1031 AA.
AC A0A2S7QT82;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=CJF32_00000393 {ECO:0000313|EMBL:PQE29737.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE29737.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE29737.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE29737.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PQE29737.1}.
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DR EMBL; NJPR01000057; PQE29737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7QT82; -.
DR STRING; 2070412.A0A2S7QT82; -.
DR InParanoid; A0A2S7QT82; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000238813; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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:UP000238813};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 670..874
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1031 AA; 116302 MW; 25C2A8DA256386B7 CRC64;
MLRNSLRQTS SQLLRGGCSA RSLCTTSRSP LSTSKATAKL SSKRCSLAAV TQKRHESTAA
NAPDPNDNFL SGNTANYIDE MYMQWKEDPS SVHISWQVYF RNMENGDMPM AQAFTPPPTL
VPTPTGGVPS FLPGLGGAEG SEVTNHLKVQ LLCRAYQARG HHKADIDPLG IRREAEQFGY
SKPKELQLEH YQFTEKDLDT EYSLGPGILP HFKKEGRDKM KLRDIIAACE RIYCGSYGVE
YIHIPDREQC DWLRARIEVE KPFKYSIDEK RRILDRLIWS SSFEAFLATK YPNDKRFGLE
GCETLVPGMK ALIDRSVDFG VKDIVIGMPH RGRLNVLSNV VRKPNESIFS EFGGSAAAED
EGSGDVKYHL GMNFERPTPS GKRVQLSLVA NPSHLEAEDP VVLGKTRAIQ HYNNDEKDHK
TAMGVLLHGD AAFAAQGVVY ECLGFHSLPA YSTGGTVHLV VNNQIGFTTD PRFARSTAYC
TDIAKSIDAP VFHVNADDVE AVNYVCQLAA DWRAEFQRDV VIDLVCYRKH GHNETDQPSF
TQPLMYKRIQ KKSPQIDIYI DQLLKDGSFT KEDIEEHRKW VWGMLEDSFA KSKDYQPTSK
EWTTSAWNGF KSPKELATEV LPHNPTGVPT HTLEHIAETI GTAPEGFNVH RNLKRILNNR
VKTVSEGENI DWSTAEALAF GSLVSEGHHV RVSGQDVERG TFSQRHAVFH DQENEKTYTP
LQHISKDQGK FVIANSSLSE FGALGFEYGY SLSSPDALVM WEAQFGDFAN NAQCIIDQFV
ASGEVKWMQR SGLVMSLPHG YDGQGPEHSS GRMERYLQLC NEDPRIFPSP EKLERQHQDC
NMQIAYMTSP SNLFHILRRQ MNRQFRKPRS SIDEFTGDSQ FKWIIPDPEH GKTINDPENI
ERVILCTGQV WAALSKYRSD NNIKDTAFTR IEQLNPFPWQ LLKENLDMYP NAKTIVWCQE
EPLNAGAWSF TQPRIETLLN NTQHHDRKHV MYAGRNPSAS VATGLKASHT KEEAELLETA
FTVTQDKLKG E
//