ID   A0A3A2ZS28_9EURO        Unreviewed;       717 AA.
AC   A0A3A2ZS28;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=PHISCL_02529 {ECO:0000313|EMBL:RJE25123.1};
OS   Aspergillus sclerotialis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Polypaecilum.
OX   NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE25123.1, ECO:0000313|Proteomes:UP000266188};
RN   [1] {ECO:0000313|Proteomes:UP000266188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA   Tafer H., Lopandic K.;
RL   Submitted (FEB-2017) 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}.
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:RJE25123.1}.
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DR   EMBL; MVGC01000057; RJE25123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A2ZS28; -.
DR   STRING; 2070753.A0A3A2ZS28; -.
DR   Proteomes; UP000266188; 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; -; 3.
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; 2.
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:UP000266188};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          375..570
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   717 AA;  78973 MW;  7BA9BA23D1BEE1A2 CRC64;
     MALTEMEANI QRDRDKNITD DELATLTLRN LIFDICNQNG GGHGGSAIGM AAIGVALWKY
     IMRYNPSNPS WFDRDRFVLS NGHCAMFLYA LNYLTGFDSW TMEELKGYAG AKLNGFTTMA
     HGHPEIECPG VEVTTGPLGQ GIANAVGLAI ASKNLSASFN EPGFDVVNSS VYCMTGDGCL
     MEGVALEAIS LAGHLRLENL ILIYDNNGTT CDGPLSWINT EDTNGKMRSC GWHVVDVIDG
     SHNVQAICAA LQHARNLRGK PVFVNVRTII GVGTSTAGTA KAHHGAFDNE SVSRSKILAG
     GDPSVTHYVT ERGLKFFREC KSHGENLEKQ WLELLEKYTY VYPDKAREFA SRRRGTFSGH
     NDLLQKIGTN SFRGMPTRES NGLVLERLWQ VCPLIGGGAD LVNSNKFLYS EADVFHPSVS
     YRGRYIRYGI REHAMASISN GLAAFHPGTF LPVTATFLMF YIYAAPGVRM GALSHLPTVH
     IATHDSFGKV LDSLTVYTER SEKTNKLTAE GQNGPTHQPV ELDSLYRAMP NLTYVRPCDA
     EEVVGAWMCA LQSTSNPTMI SIARDPAGEV PNTNRLLTLR GAYVIDEDVN ADLTLVSCGS
     NLHHVVVAVK QLRQESIRCR IVSCPSFDLF DRQTEEYRQS VFPLNGKAIV SVEEYVATTW
     ARYVTASIGM KTYGYSASNE SNYERFGLDA KGIVSRIKSY MLFLDGRNAR QMGWRSI
//