ID   A0A0C3P1L2_PISTI        Unreviewed;       959 AA.
AC   A0A0C3P1L2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=M404DRAFT_1003077 {ECO:0000313|EMBL:KIO01381.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO01381.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO01381.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO01381.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN831988; KIO01381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3P1L2; -.
DR   STRING; 870435.A0A0C3P1L2; -.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; A0A0C3P1L2; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000054217; 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:UP000054217};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          600..803
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   959 AA;  106166 MW;  BFFD0E42232AF87D CRC64;
     MILARNTPTW LYLAKRSQPT ATSKGRVIAF RRAYHDESFG FRRPRQFTMP DYTPAELRNR
     AVNAPLLRYA DALRTHGHRA ASIDPLDLLR RERVPALEPE RYGLPDPNAV YDTSGILWTG
     RESESNTQWA LRDITEFLNA VYVGRIAYEY MDLPSRTERL WFAHLLESQS STSMLHCNAE
     RKQRIHQLIA CSEVLDTFLQ AKFPNLKRYG LEGGESMLPA LDALIGEAAR AGITRVVLAM
     PHRGRLNLLT GLLGYDPAAL FYKIKGGAEW SVQGGQFAGD VLSHLVASPT LNYDGKEIKV
     SLLPNPSHLE AVNPVALGKA RAKQYTLLKA LEKGGKGAEG CMLGDKVMCV QLHGDASFTG
     QGIVMETLGL SNLPHYTSGG SVHIVVNNNI GYTTPASSAR SSLYCSDVAK MINCPVLHVN
     GDYPEDVVRA VEIAFKYRNY FRKDVVIDLL VYRRWGHNEL DEPSFTQPLM YQKIRARRSV
     PALYEDKLVN EGTLEEDTAA SVRASCKATL TDALAASASY SPPLIKLEGQ WNATQIDNND
     VKMVWPGSPE AQTFDTGVDA EVLREVGSAS VSVPDGFEIH PRLQRHVKSR LAALEKGEGI
     DWATAEAMAF GSLMLGGCDV RIAGQDVGRG TFSHRHAMLV DQKTEGVIVP LNHALSRATG
     KLELANSSLS EEAVLGFEYG ASWERPDFLP IWEAQFGDFF NGAQVIIDTF ISSAETKWAK
     QSGIVLLLPH GLDGAGPEHS SSRIERMLQL TNDAYSPQPN TNVNMHVVYP TTPAQYFHLL
     RRQLKRNYRK PLVVAAPKGL LRLAAASSRL VDMLPGTKFH PVIPDNAPTN TAKRVILMSG
     KLYYDLVKER TARNLDEHVA IIRIEELAPF PFSELTDVLK LYTSNGTKRV EWMWVQEEPK
     NQGAWGHVKD RLEVVLRALV GDGNVVYVGR REDAVPAPGV GETYRAQQKA VMDGAFSGL
//