ID A0A0D7BPI0_9AGAR Unreviewed; 917 AA.
AC A0A0D7BPI0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000313|EMBL:KIY72322.1};
GN ORFNames=CYLTODRAFT_388972 {ECO:0000313|EMBL:KIY72322.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY72322.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY72322.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY72322.1,
RC ECO:0000313|Proteomes:UP000054007};
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; KN880445; KIY72322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BPI0; -.
DR STRING; 1314674.A0A0D7BPI0; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000054007; 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:UP000054007};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 567..770
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 917 AA; 102638 MW; F1FFE39C1CCB32DE CRC64;
MLSKHLSTRL RTATPRRLYH DESFGYRAPR SYQFTDYTSA QLANRSENAA LLRYVDSVRT
HGHRAARIDP LDLIHRMEVK ALDPHRYGLY DDEKKYNVNG IIWTNPKVET QGENQDEWWT
LGEITRHLRS IYVDKIAYEY MHSPSKSERL WFSHHLEGNA SSPHIDQRRI HGLLARSEVF
DNFLQLKFPN LKRYGLEGGE SMLPALDTLF SCAAHASMSN VIVAMPHRGR LNLLTDLLAF
SPTALFHKIR GGFELPEELG AEGDVISHLT SSADLAGVKV SLLPNPSHLE AVAGVALGKT
RAKQYSLLKT SPDDCMLGDR VISCQIHGDA AFAGQGVIME SLGLSNLPHF SSGGTVHLVV
DNNIGYTTPA SLARSSQYCS DVGKMINAPV LHVNGDYPED VVRAMEIAFK YRQYFRKDII
VDLLVYRRWG HNELDLPGLT QPLMYEAIAA RRSVPQLYEQ RLLDQQTITV KDVTEVRDSY
KAFLNDQLSQ VDGFRPSANM LQSQWKSMVW PASPEANDNP KDTGVDVDVL KSVGQASVRV
PDGFAIHPKL QRHIKSRLTS LEKGQGLDWA TAEALAFGSL LQEGYDVRIS GQDVGRGTFS
QRHAMLVDQA KEDTIVPLND ELKAKGKLEL ANSSLSEMAV LAFEYGASWE RPDLLPIWEA
QFGDFFNGAQ IIIDTFISSS ETKWLKQSGI VMLLPHGLDG AGPEHSSSRL ERMLQMSNDR
FSSSETKPNI NMHIVFPTTP AQYFHLLRRQ MKRNYRKPLI VAGPKGILRL SAAGSSIDQL
APGTAFQPVL LEDKPVSDPK RIVFLSGKLY YDLVKERATR KLDDSVAFVR IEELSPFPFN
AVAEVAKAHP EAECVWVQEE PRNQGAWSFV RDRIEDVLDG RRLRYVGRKE SAVPAPGVGV
LYKKQQADVL AGAFKGL
//
