ID   A0A1Y1WEA4_9FUNG        Unreviewed;      1013 AA.
AC   A0A1Y1WEA4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000313|EMBL:ORX71576.1};
GN   ORFNames=DL89DRAFT_256573 {ECO:0000313|EMBL:ORX71576.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX71576.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX71576.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX71576.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORX71576.1}.
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DR   EMBL; MCFD01000004; ORX71576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1WEA4; -.
DR   STRING; 61395.A0A1Y1WEA4; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000193922; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000193922};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          605..809
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          539..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  112501 MW;  62376F0ED00BF224 CRC64;
     MLKAGNSARR AVLPQIVRSA SLFRCLSPRA IRKASNRLQP ILILANRYHE GAEYGNLAPP
     QVEPKGCTQK EWNFGSFTPE ELRNRQQQPE LLHLVNAYRR HGHLSSNLDP LGIKKAELIE
     ELSGGFYGLN EESKAYNIEG VIAPSSGLSR RADLSAIIEA LQRTYCRNIS YEFEHITSPA
     VRQWFAGYVE SLDTADISLR RERFFEHMTK AEAFEQFVQK KLPNVKRYGL EGSESMAVLL
     DQLIFEGSCA GMADTVLGLS HRGRVTLMAT MFGYSEAEVF HKLRGGSEFP NGSPHTGDFI
     VDLTKPAVVT FPETNVPMNI DIVHNACHLE SGSPVALARA AQRTSILRKP ADLTDIQSAT
     MCWPSVFMAT LFAGQGIVAE TLGMSGLAHF TNGGTIHIVL NNQVGYTTPA SHARSTRYAS
     DIAKFADIPI IHVNGEHPEE VARAARIAFA YRSKFRKDVV IDMWTFRTRG HNEMDEPTFT
     QPAMYKAIHG RKSIPAQFEE RLINDGVLTS DYASAFRKSY INTLNMAFAQ SLNCNPTEAP
     KSPRWRMLSP PRSLPVEKPT GVDIGTLKEV GLQSVTPAKG CKVHPRIERF HIKPRVKRLN
     EDQPVDWATA EAMAFGTLLK EGYHVRLSGQ DVGRGTFSQR HAMLVCQDTE QISVPLNLLP
     GKDAGKIEVV NSNLCEEAAL AFEYGVSVED PFTLAIWEAQ FGDFFNNAQT QIDGYVTSGE
     TKWGQQNGLV VLLPHGFDGG GPDHSSCRLE RHLLLSNDPV DGNPGQAMPN VYIAFPTTPA
     QMFHLLRRQM KRNFRKPLIV AGPKTLLRLA QAVSPLSDMG PGTQFQPVLD DPVVQDPRAV
     RRVMLVSGKL YYDLAKLRSE HPLGEHVAIV RVEELSPFPR QQLYQTISQY TNATDFVWVQ
     EEPRNAGAYS FMAQRVTQLL PEYAPQLRYV GRDEHAAVCS GVDSQQAEEH VRLTREAFEG
     LRSLVVDLAA ESSASQIRHR QLEDSAHSAV MPAIAHRWGE GGRIHAAQGV ADQ
//