ID   A0A135SBY3_9PEZI        Unreviewed;       926 AA.
AC   A0A135SBY3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Oxoglutarate dehydrogenase {ECO:0000313|EMBL:KXH33425.1};
GN   ORFNames=CNYM01_05061 {ECO:0000313|EMBL:KXH33425.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH33425.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH33425.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH33425.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH33425.1}.
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DR   EMBL; JEMN01001564; KXH33425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135SBY3; -.
DR   Proteomes; UP000070054; 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; 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; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          558..767
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   926 AA;  102314 MW;  78B492DC05EF43AC CRC64;
     MEDPSVHSTQ AFQPPPGIIS PRHTPPIKSS LGADSSHVVD SLKTQNIVRA FQRHGHSAAK
     ISPLGEVGNA TVKPHDDIPS TTNLSKYGFT SADLDREIVL GPELLPHLAQ DHKTMKLRDI
     IATCEKIYCG SIGAEYHHVS DPTKRQWLRE RIEAYHTSPP SREEKKQILD NLIWATSLER
     FLAAKFPNKK RFGLDGAEGL APGLAALIDR CAEAHGVQDI VIGSCHRGRM NLMSTVYGKD
     YETLFRQFAG TEAFDTAKGQ TGDVKYHFGM EDERATAGGK TVGISMLPNP SHLEAIDPVA
     QGKAKAVQHL NNDVDQSKVM FLALHGDAAF SGQGPVYETL NLSALKGYEV GGTIRIIVNN
     QIGFTTDSPD SRSTPYCTDL AKYIEAPIFH VNADDPEAVV FISKLAADWR AEFRSDIVVD
     VVCYRRFGHN EIDQASFTQP EMYKRIAEQR SLMDLYIEKL IGEGVMSTEM TERQKTWVWE
     QLEEKLARSK QPADRPLDIA ASDLTSAAHT TPSAIAVEVA ALSTITNAIT SVPEGFNLHR
     NLQRILAAKK QAFDEGTVDW STAESLAFGT LLQDGKSIRL SGQDVERGTF SQRHSVLHDQ
     VTHEEYTPLN NLDTPGAGTY SAINSPLSEF GVLGFDYGYS LAARDSLVIW EAQFGDFVNN
     AQVIVDQFIS SGEAKWMLES GLVMSLPHGY DGQGPEHSSA RLGRFLELGS EDGRAWPEDL
     ERANREGNIR IVCMTTPANL FHALRRQVYS PEKKPLIIFF SKSLLRHPIA RSSVSDLTGS
     STFQPVLEDP EHGRDNILPR EEIGRVILCS GQVYAALHKY REAKGIKNVA ITRIEELHPL
     PWAQVKENLE SYPNTQKIVW CQEEPYNGGA WQYMRDRLET VIENSSVLGG KKIVYAGRGT
     GAATATGSKK VHQAEETKLL EDAFEG
//