ID   A0A1F7ZNL3_9EURO        Unreviewed;       697 AA.
AC   A0A1F7ZNL3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=ABOM_010230 {ECO:0000313|EMBL:OGM41047.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM41047.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM41047.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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:OGM41047.1}.
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DR   EMBL; LYCR01000122; OGM41047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7ZNL3; -.
DR   STRING; 109264.A0A1F7ZNL3; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000179179; 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:UP000179179};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          375..550
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   697 AA;  76039 MW;  D047CC3D6BE36CC0 CRC64;
     MTIPNQQSNM KRTSLSDNDQ AVTDLRRLII DCCRQNGGGH GGSAIGMVPL AVALWRHTMR
     FNPRNPEWFD RDRFVLSNGH AAILLYIMLH AAGYPEMTMD ELRKYASPKT PDRNGQWEAT
     LCHGHPEIEV PGVEVTTGPL GQGIANAVGL AIASKHLAAV FNKPGHRVIS SKIYCTTGDG
     CLQEGVAQEA MAIAGHLGLD NLILCYDNNQ VTCDGPLSWI VSEDTNSKMR ALGWNVLDVW
     DGDDSVEEIL AALRLAQMST SKKPTFINIR TTIGYGTSRA GTFRSHHGTY TDEDAARFTN
     GDGDSVSHCL SQQTRDFFLP LIEQGNVLES GWNELVSTYA ESFPQDAQHL RSRISGQLDV
     QDLLKTMNPN VGDPLATRQW NGAVFNTLMD NVSSMVAGGA DLWNSNQMGD QSSRILGRDH
     YAGRVVRYGI REHAMAAISN GIAAFHPGSF IPVTATFLMF YLYAAPGVRM GALSHLRVIH
     VATHDSIGEG QNGPTHQPVE VDSLFRAMPN LLYIRPADEE EVIGAWMCAL GNENKNVPSI
     ISLARDPPSV RIPTTSRDSV ALGGYVVLEL DNALVTLVSC GSELQCAVMA ARKLAGELGI
     PTRVVSMPCI SLFEKQAETY QKAVLSDSPH IVSVEAYVST IWARLCTASI SMDSFGYSGA
     GSANFRRFGL DGDSIARKIQ RHVQSTHVTA KRWVRLE
//