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
//