ID A0A094DNP5_9PEZI Unreviewed; 1070 AA.
AC A0A094DNP5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-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=V496_05149 {ECO:0000313|EMBL:KFY61095.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY61095.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY61095.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY61095.1}.
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DR EMBL; JPJY01000900; KFY61095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DNP5; -.
DR STRING; 1420909.A0A094DNP5; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000029302; 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:UP000029302};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 694..904
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 120240 MW; C5B49309288A1D9C CRC64;
MTADKSSSGS PDCRWLERDE KARTSFRKSS SQLLRAGCQA RSLSANSSSR ATIFSSPSPL
KSSIASKRRP LAVASQKRYA AAVANAPEPN DSFLSGNTAN YIDEMYMSWK EDPSSVHVSW
QVYFRNMESG DMPMSQAFTP PPTLVPTPAG GVPSFMPGSA TGPGNDVTNH LKVQLLVRAY
QARGHHKARI DPLGIRGEAK EFGYSNPKEL HLDHYGFTEK DLDSEYTLGP GILPRFKKDG
REKMTLREII AACENIYCGS YGVEYIHIPD REQCDWLRER IEIPQPYKYS VDEKRRILDR
LIWSSSFEAF SATKYPNDKR FGLEGCETLV PGMKALIDRS VDYGVKDIVI GMPHRGRLNV
LSNVVRKPNE SIFSEFGGTA AGEDEGSGDV KYHLGMNFER PTPSGKRVQL SLVANPSHLE
AEDPVVLGKT RAIQHYNNDE KNHTTAMGVL LHGDAAFAAQ GVVYECLGFH SLPAYSTGGT
IHLVVNNQIG FTTDPRFARS TAYCTDIAKA IDAPVFHVNA DDVEAVNYVC QLAADWRAEF
RSDVVIDLVC YRKHGHNETD QPSFTQPLMY KRIQDHEPQI DIYVNQLLKD GTFTKDDIDE
HKQWVWGMLE ESFAKSKDYQ STSKEWTTSA WNGFKSPKEL ATEVLPHPPT GVKKETLEHI
GTAIGTAPEE FNVHRNLKRI LANRVKTVNE GQNIDWSTAE ALAFGSLVTE GHHVRVSGQD
VERGTFSQRH AVFHDQEDET TYTPLQHVSK DQGKFVISNS SLSEFGCLGF EYGYSLTSPN
ALVMWEAQFG DFANNAQCII DQFIASGEVK WMQRSGLVMS LPHGYDGQGP EHSSGRMERY
LQLSNEEPRV YPSQDKLDRL HQDCNMQIAY MTSPSNLFHI LRRQMNRQFR KPLIIFFSKS
LLRHPLARSS IDEFVGDTQF RPIIPEQEHG GAAVEPKDIK RVVLCTGQVY AALHKHRLDK
GITDTAITRV EQLNPFPWQQ VKENLDSYPN AETIVWCQEE PLNAGAWTFT QPRIETILNV
TEHHNRKHVM YAGRNPSASV ATGLKASHLK EESELLEMAF EVRQEKLKGE
//
