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Database: UniProt
Entry: A0A0D7AN24_9AGAR
LinkDB: A0A0D7AN24_9AGAR
Original site: A0A0D7AN24_9AGAR 
ID   A0A0D7AN24_9AGAR        Unreviewed;       956 AA.
AC   A0A0D7AN24;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000313|EMBL:KIY53250.1};
GN   ORFNames=FISHEDRAFT_63426 {ECO:0000313|EMBL:KIY53250.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY53250.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY53250.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY53250.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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}.
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DR   EMBL; KN881627; KIY53250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7AN24; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000054144; 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   Reference proteome {ECO:0000313|Proteomes:UP000054144};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          599..804
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   956 AA;  107043 MW;  EE03C7C565069B3F CRC64;
     MPTGTVSPRG CRVPRFHSHA AFHTQTPDLE SSPHPNRCAV LIRRSYHDES FGFRKPREHT
     FPDYTEAQLK NRHLNAPLLR YVDSVRMHGH RAARIDPLNL VPRLEVAALN PARYGLVDEQ
     KPYDVNGIVW TAPVGANVEE HDRAQMWTLG EIISYMRTIY VDRIAYEYMH SPSKTERLFF
     SKLLESSSVS PVTTDEKRRM LELIIRSETL DNFLQLKFPN LKRYGLEGGE SMIPALDTLF
     SVASRAGIEH IVLCMPHRGR LNLLTELLEF PAAALFAKIT GGSELPEAYG GEGDVLSHLS
     ASPELQYDDA VKPVRVSLLP NPSHLEAINP VALGKARAKQ YTLLKTSPPS CTLGDRVMCV
     QLHGDASFTG QGIIMEGIGL SNLPHFTSGG SVHIVVNIGY TTPAAGARSS MYCSDIGKMI
     GAPVLHVNGD YPEEVAKAME IAFEYRNYFR KDVIVDLLVY RRWHNELDLP DFTSPLMYDM
     INSRRSVPAL YEEKLTTEGI AEEGTGKRIR DNYKEYLQSQ LVQAETYTPS PVVLQGQWSD
     MVWPTDCDAF HNPATGVSTD VLKEAGHASI YVPEGFTVHP KLNRHIKHRL QGLDSEQQLD
     FATAEAMSFG SLLREGYDIR ISGQDVGRGT FSQRHAMLVD QKTEQVIVPL NDRLAAPGKL
     ELANSSLSEF AVLGFEYGVS WERPTLLPIW EAQFGDFFNG AQIIIDTFIS SAETKWLKQS
     ALVLLLPHGL DGAGPEHSSS RIERMLQLTN DPFEYPHDNI TPNVNMHVIF PTTSAQYFHL
     LRRQMKRNYR KPLIVASPKG LLRLPAASSS LADMALGTAF QPVIDDATVE PSNVARVVLV
     AGKFYYELSK ERVTLNRQDV ALVRIEELCP FPFISLRAVL ARYPRAKDYL YVQEEPRNQG
     AFPHVRERAN AVLDAMFPGQ HRKVRYVGRC ESAVPAPGIA KLYTTEQRAV LLEAFA
//
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