ID   A0A0L6UQU3_9BASI        Unreviewed;      1115 AA.
AC   A0A0L6UQU3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000313|EMBL:KNZ50896.1};
GN   ORFNames=VP01_418g3 {ECO:0000313|EMBL:KNZ50896.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ50896.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ50896.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ50896.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) 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:KNZ50896.1}.
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DR   EMBL; LAVV01009268; KNZ50896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6UQU3; -.
DR   STRING; 27349.A0A0L6UQU3; -.
DR   VEuPathDB; FungiDB:VP01_418g3; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000037035; 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; -; 2.
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   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; 3.
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:UP000037035};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          687..904
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1029..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1115 AA;  124225 MW;  3C7C34DF09C5B568 CRC64;
     MALQLRVRPK LFLRGSFRLV TRAFQHSSAV DPPVWGYQRP ESFQLPDFTP QQLYNRASQA
     SLVRLVDSYR VTTSNHELVP SSCIWSNKRH AHRSATLDPL SLTPRPSVSA LDPRRYGFGV
     SSSFLQDRLH SNHITHDLPS EMLEHLGDET KLWAVDGVVG MGTRTPGGLQ RTLGEIVDRL
     QEVYCGRIAY EYMHLPNKSE REWLSDTLES KVHDMSISQD CKLHYWQLLY RSEAFDKFLG
     AKFPNVKRYG LEGGESMLVA LDRIFEECSV HGVKDVVVWR HAPSRSPQFL DSTAIIGPSD
     PVEEGAHLAH IVPLEGKTEI SKKLLRDTPA YTGDVLSHLT TSTALQSRSH PRGQPVNVHV
     LPNPSHLEAV SPVGLGVARA LNMLDGARPY IESLSVNDKR IGDEVLSVQI HGDAAFGGQG
     VVAETLNLSE LVSPLNITRR RLPLVQMFSD DTLSSTCQGT LPHFTVGGSV RLVLNNQLGY
     TTPATEGRTS FYATDIGKSI SAPIIHVNGE YPEDVSRALS LAFAFRNQFR KDVLIDLVVY
     RRWGHNDPHM YRKIESLPSV PTCYEKELVN SRQFDVQTLS KIKSTINQEF SQALDVQLTS
     NRNHDEGKTG LMDLENIVRN RPYPSHKSRR ISEEAETGVS LERLQAAGRA SVSTPKDFNV
     HPRLQKMHIR KRLQALENKS EFSKPAIDFS TAEALAFGTL LEDGFDIRLS GQDSGRGTFS
     QRHALLTDQS VEGRTVVPLN ELAIHDPGRG KLEIVNSPLS EYSVMGFEIG FSYMTSRSCL
     VLWEAQFGDF VNTAQVIVDH FLASGQFKWP TFQSGLVLLL PHGLDGAGPE HSSCRIERFL
     QAANEPWLFR DRATQVGHEG ENISICNATT PAQYFHLLRR QMKTARTKSP KGLIICTPKT
     MLRARETFSS LTELGLGTAW KEVLDDPLME KNPSTKDSVE RLVICSGKVY YDLAKKRHSL
     GLDSTVALVR IEELTPFPYR SLHQVMRSYP SIKTVIWAQE EPENAGGLSF VAHRIREVVH
     NLGNPASFLR AADGQAPPGD GGHESDNKGG HSFSSLTCMA LHAHTKGYTH TVIKIGFVSR
     PACASSSTGI SEQFKNQQSH LESQVFDFNH APRPL
//