ID A0A1Q8RYP6_9PEZI Unreviewed; 1042 AA.
AC A0A1Q8RYP6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CCHL11_01620 {ECO:0000313|EMBL:OLN92224.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN92224.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN92224.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN92224.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) 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:OLN92224.1}.
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DR EMBL; MPGH01000060; OLN92224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RYP6; -.
DR STRING; 708187.A0A1Q8RYP6; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000186583; 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:UP000186583};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 665..875
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1042 AA; 117016 MW; 0BC3D9EC07B0656B CRC64;
MFASTRAARN GAAAVRSLVA TSRVAVRSPA LTSPTVRSAA RPIALTTRRH YASAADSAPP
NPNDNFLSGN TANYIDEMYI QWKQDPKSVH VSWQVYFKNM ENGDMPISQA FTPPPSLVPG
ATGGVPGLAA GLGQGSEITN HLKVQLLVRA YQARGHHKAN IDPLGIRNES KGFGNIKPKE
LSLEHYQFTE KDLDAEYELG PGILPRFKKE GRDKMTLREI IAACEKIYCG SYGVEFIHIP
DREKCDWLRE RLEVPQPFKY SIDEKRRILD RLIWSSSFES FLATKYPNDK RFGLEGCESL
VPGMKALIDR SVDYGVKDIV IGMPHRGRLN VLSNVVRKPN ESIFSEFAGT AGAEDEGSGD
VKYHLGMNFE RPTPSGKRVQ LSLVANPSHL EAEDPVVLGK TRAIQHYNND EKTHRTAMGV
LLHGDAALAG QGVVYECLGF HSLPAFSTGG TIHLVVNNQI GFTTDPRYSR STPYCTDIAK
AIDAPVFHVN ADDVEAVNFV CQLAADWRAE FQQDVIIDLV CYRKHGHNET DQPSFTQPLM
YKRIQSHESQ ISIYVKKLLE DGSFTKEDID EHKQWVWGML EDSFSKSKDY QPTSKEWTTS
AWNGFKSPKE LATEVLPHLD TSVDSKTLQH IGEVVGNAPE GFNVHRNLKR ILANRTKSVV
EGKNIDFPTA EALAFGSLVT EGHHVRVSGQ DVERGTFSQR HAVFHDQETE DTHTPLQNVS
KDQGKFVISN SSLSEFGALG FEYGYSLSSP NALVMWEAQF GDFANNAQCI IDQFIASGEA
KWMQRTGLVV SLPHGYDGQG PEHSSGRLER WLQLCNEDPR VFPSPEKLER QHQDCNIQVV
YMTSPANLFH VLRRQMHRQF RKPLIIFFSK ALLRHPLARS DIEEFTGDSH FKWIIPDPEH
ETGAIKPKEE IDRVILCSGQ VWATLSKYRA DNKIDNVAFT RVEQLNPFPW QQLKENLDQY
PNAKTIVWCQ EEPLNAGAWS FTQPRLETLL NQTEHHDRKH VMYAGRGPSA SVAAGTKGLH
TKEEQEFLEM AFTVKQDKLK GE
//
