ID A0A2P7YJ24_9PEZI Unreviewed; 1052 AA.
AC A0A2P7YJ24;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=B9Z65_5791 {ECO:0000313|EMBL:PSK35976.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK35976.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK35976.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK35976.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) 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:PSK35976.1}.
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DR EMBL; NHZQ01000422; PSK35976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YJ24; -.
DR STRING; 40998.A0A2P7YJ24; -.
DR Proteomes; UP000243723; 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:UP000243723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 671..881
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1052 AA; 118593 MW; 0E4CBA17580A1AAC CRC64;
MLLSALRQCN RRLLGANSGT RASLSTYNTA RPASALISKR RDLAITQHGS ARRGYAVAAE
ETSKGVDPND SFLQGNTANY IDEMYMEWKN DPTSVHVSWQ HYFKNMESGN MPISQAFQPP
PSIVSQPTGG VPALTETSMG SSDVSAHLKV QLLVRAYQAR GHHKAKIDPL GIQNEASKFA
TSDPKELNIE AYKFSEQDME QEYELGPGIL PRFKTADRHK MKLKDIIAAC EKLYCGSVGV
EYIHISDREQ CDWLRERIEV PEPYKYSVDE KRRILDRLIW SSSFESFLAT KYPNDKRFGL
EGGESLIPGM KALIDRSVDH GVKDIVIGMP HRGRLNVLSN VVRKPNESIF SEFGGSAEPS
DEGSGDVKYH LGMNFERPTP SGKRVQLSLV ANPSHLEAED PVVLGKTRAI LHYNNDEKEA
TSAMGVLLHG DAAFAGQGVV YETMGLYALP SYHTGGTIHI VVNNQIGFTT DPRFARSTPY
CSDIAKSIEA PVFHVNGDDV EAVNFVSQLA SDWRAEFKKD VVIDIVCYRK QGHNETDQPS
FTQPLMYKRI GEQKPVLDKY IDKLIEDKTF TKDDVDEHKK WVWGMLEDSF SRSKDYQPTA
KEWLTSAWNG FKSPKELATE VLPHLPTAVE ADTLKQLGEA IGNPPKGFNV HRNLKRILAN
RAKTVNEGKN IDMSTAEALA FGSLCLEGHH VRVSGQDVER GTFSQRHAVL HDQETEETYV
PLKNIGKDQG SFVISNSHLS EYGVLGFEYG YSLSSPSALV MWEAQFGDFA NTSQVIIDQF
VASGEVKWMQ RSGLVMNLPH GYDGQGPEHS SGRMERFLQL CNEDPRIFPS PEKLDRQHQD
CNMQVAYCTT PSNTFHLLRR QMNRQFRKPL ILFFSKSLLR HPLARSNIED FTGDSHFQWI
IPDPAHNEGQ DIQIKPHDQI ERIIICTGQV YAQLHKHRTQ HNYTDTAITR IEQLNPFPWA
QLKENLDSYP NAKTIVWCQE EPLNAGAWSF TQPRIETLLN QTEHHNRRHV LYAGRNPSAS
VATGLKSSHM KEEQDLLDMA WRVKQDKLKG EA
//
