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Database: UniProt
Entry: A0A0D9N7T4_ASPFA
LinkDB: A0A0D9N7T4_ASPFA
Original site: A0A0D9N7T4_ASPFA 
ID   A0A0D9N7T4_ASPFA        Unreviewed;       810 AA.
AC   A0A0D9N7T4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   SubName: Full=Putative phosphoketolase {ECO:0000313|EMBL:KJJ36177.1};
GN   ORFNames=AFLA70_43g003540 {ECO:0000313|EMBL:KJJ36177.1};
OS   Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392242 {ECO:0000313|EMBL:KJJ36177.1, ECO:0000313|Proteomes:UP000032444};
RN   [1] {ECO:0000313|Proteomes:UP000032444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-384 / AF70 {ECO:0000313|Proteomes:UP000032444};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus flavus AF70.";
RL   Submitted (FEB-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 XFP family. {ECO:0000256|ARBA:ARBA00005623}.
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:KJJ36177.1}.
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DR   EMBL; JZDT01000108; KJJ36177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9N7T4; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000032444; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02011; TPP_PK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   HAMAP; MF_01403; Phosphoketolase; 1.
DR   InterPro; IPR023962; Phosphoketolase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
DR   InterPro; IPR018969; Xul5P/Fru6P_PKetolase_C.
DR   InterPro; IPR019790; Xul5P/Fru6P_PKetolase_CS.
DR   InterPro; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR   InterPro; IPR019789; Xul5P/Fru6P_PKetolase_ThDP_BS.
DR   PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR   PANTHER; PTHR31273:SF0; PHOSPHOKETOLASE-RELATED; 1.
DR   Pfam; PF03894; XFP; 1.
DR   Pfam; PF09363; XFP_C; 1.
DR   Pfam; PF09364; XFP_N; 1.
DR   PIRSF; PIRSF017245; Phosphoketolase; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          27..387
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          605..805
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   810 AA;  91488 MW;  9A0E61733CDDE24F CRC64;
     MAPSSESDDN ISAYGATRST IKGQPLDADE VRKMDAYFRA SMYLCLGMLY MRDNVLLKEP
     LKVEHLKARL LGHWGSDAGQ SFTWLHMNRL IKKYDLDVLF VSGPGHGAPA VLSQSYLEGV
     YSEVYPDKSE DEKGLQRFFK QFSFPGGIGS HATPETPGSI HEGGELGYSI SHAFGSVFDH
     PNLITLTMVG DGESETGPLA TSWHSTKFLN PCTDGAVLPV LHLNGYKINN PTVLARISHE
     ELKALFVGYG WTPYFVEGND RESMHQAMAA TLEHCIVEIK KIQKQARESN KPFRPCWPMI
     VLRSPKGWSA PREIDGKLLE GFWRSHQIPI TDVLTNPAHL KLLETWMKSY KPEELFDKNG
     KLVEELKALA PSGNSRMSAN PVGNGGILRR PLQLPDFRDY ALKDIDPGVS VRGSMTNMSK
     FLRDVVKENM TTFRVFGPDE TESNKLAEIY KAGKKVWLGD YFEEDKDGGN LAFEGRVMEM
     LSEHTCEGWL EGYVLSGRHG ILNSYEPFIH VIDSMVNQHC KWIEKCLEVE WRAKVASLNI
     LLTATVWRQD HNGFTHQDPG FLDVVANKSP EVVRIYLPPD GNTLLSVMDH CFRSVNYVNV
     VVADKQEHIQ FLSMDEAIEH CTKGLGIWDW ASNDQGQEPD VVMAACGDVP THEALAATAL
     LNEHLPQLKV RFVNVVDLFR LINEKDHPHG MPDRQWKAVF TDDKPIIFNF HSYPWLIHRL
     TYKRPGQHNL HVRGYREKGN IDTPFELAVR NQTDRYSLAI DAIDRVGSLG NTASHAREKL
     INQQLAAKQE AYDNGLDAEY IRNWKYPKKA
//
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