ID   A0A0D2CA06_9EURO        Unreviewed;       703 AA.
AC   A0A0D2CA06;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=PV06_02328 {ECO:0000313|EMBL:KIW46677.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW46677.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW46677.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW46677.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; KN847333; KIW46677.1; -; Genomic_DNA.
DR   RefSeq; XP_016266893.1; XM_016402996.1.
DR   AlphaFoldDB; A0A0D2CA06; -.
DR   STRING; 215243.A0A0D2CA06; -.
DR   GeneID; 27354402; -.
DR   VEuPathDB; FungiDB:PV06_02328; -.
DR   HOGENOM; CLU_009227_0_0_1; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF6; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          382..556
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  76565 MW;  36237C848B384D9C CRC64;
     MSSNTATNGS IEHTIDAPTS RRHGHDDDQQ AVREIRKLII DCCRQHGGGH GGSAIGMAPL
     AVALWRHTMR YNPRNPAWFD RDRFVLSNGH AAILLYTMLH VTGYSDMTID QLKLYASAKE
     VDPETGLWTE TLCHGHPEIE VPGVEVTTGP LGQGIANAVG LAIASKHLAA TFNRQGHEIV
     TSRVFCTTGD GCIQEGVAQE AIAIAGHLRL DNLILCYDNN GVTCDGPLDW ILSEDTNAKM
     VAMGWRVIDV FDGDSSVENI IAALRLAQSP TPDAKPTFVN IRTTIGYGTS TAGTFRSHHG
     TYSDEDAALY AEGISTHTLS KRAKQHFEWC VSSGESLEAS WNEKLAKYCE AFPAQGQQLQ
     ARIRGDLNFG SLKSLKVRNE IQATRQWNGQ VFNKLMSEVP SLMAGGADLW VSNQLGDQSK
     RIFDRANPQG RVIRYGIREH AMASISNGIA AYSHQTIVPV TATFFMFYLY AAPGVRMGAL
     SGLKVIHIAT HDSIAEGQNG PTHQPVELDS LYRAMPSLCY VRPADAEEVI GAWLVALSAK
     NQPTMISLAR DPATTAIPNT DRFKVAKGGY VVVERDDALV TLVSCGSDLQ HAVGAAAQLS
     SSGLPTRVVS MPCIDLFEQQ TNSYQDEILS KSRHIISVEP YVSTIWARYC TASVAMDSYG
     YSGAGPANMT RFGLDASGIV RKVMEHIYHN GKDSSARRWT LLK
//