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Database: UniProt
Entry: A0A2S7QT82_9HELO
LinkDB: A0A2S7QT82_9HELO
Original site: A0A2S7QT82_9HELO 
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
//
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