ID A0A066VWN6_TILAU Unreviewed; 992 AA.
AC A0A066VWN6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000313|EMBL:KDN44708.1};
GN ORFNames=K437DRAFT_268701 {ECO:0000313|EMBL:KDN44708.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN44708.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN44708.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN44708.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-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:KDN44708.1}.
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DR EMBL; JMSN01000049; KDN44708.1; -; Genomic_DNA.
DR RefSeq; XP_013242882.1; XM_013387428.1.
DR AlphaFoldDB; A0A066VWN6; -.
DR STRING; 1037660.A0A066VWN6; -.
DR GeneID; 25266047; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; A0A066VWN6; -.
DR OMA; TPAQYYH; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000027361; 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:UP000027361};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 607..825
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 992 AA; 109348 MW; 098771C16693E6CF CRC64;
MLLTNRMRGA CRLAAGNSSI VGRACGRVTA SRSYAGKGAF GFLPPPALTI EDYTPEELAN
RNANAPLLRY VDNVRRHAHR AALIDPLDLM PREDTVRALS VERYGLLESK QGHAERYDTS
GILRMPPVFA DSEAQAGTGM RSIAEITEWL RKVYVDKLSV EFMHTGMKGV RNYIMDLFED
VNTHAPLSKD EKRRCLELMT RSEVLDRFLA QRFPNVKRYG NEGAESTLPA LDMLFRKSAE
AGISSVVLCM PHRGRLSLLT ELLGMPLPSL FHKMRGGSEI PTVDSMTGHE LAGATADVLS
HLVHEPTLRY GDKDIKICML QNPSHLEAVN PVAMGKARAR QTFGKLSASD SDKGVARLGD
DVLCVQIHGD AAMSGQGIVM ESLGLSELPH YNVGGSIHLV VNNNIGYTTP STAARSSLYA
SDIAKMIGAP VLHVNGDHPE EVVKAIKIAV QMRMRFRRDV IVDLITYRRW GHNELDEPRF
TQPKMYEKIA SRASVPEAYE HRLLSESILS ADEASTLRLK RVGEMEAALA ETDQYDPTAD
HLQGKWSVCV WPTSTDAVHE PETGLEPDVA RSIGEASVAV PDGFNLHSRL NRHIKQRVES
LKEGKGINWA TAEAIAFGSL LSEGTHIRLS GEDVQRGTFS QRHAALVDQK TESIHVPLNL
ADLAASSTAK PPQGRLELAN SSLSEEAVLG FEVGVSWDRP DVLPIWEAQF GDFFNGAQVI
IDTFIAGGEA KWLKQSALTL LLPHGFDGAG PEHSSCRIER FLQLCNDPFE PPGHVVGSSS
LPYSPSLPFI NPTTPAQYFH ALRRQMKRNY RKPLIIAAPK GLLRSPHAAS TLQDFAPGTR
FQSVLDDPRF SADASQVEKM VLCSGKHYYT LVEQRAAMKL DEHVALVRLE ELSPFPFEQL
RSVLGRYKHL FAAASEVGSN ASGPHIVWAQ EEPRNQGAWV HVSLRLQALL DEVGASGLRL
AYRGRKECAV PAVGVSKWHK KEVEEMMADV FK
//
