ID   A0A137QEY7_9AGAR        Unreviewed;       659 AA.
AC   A0A137QEY7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Putative phosphoketolase {ECO:0000313|EMBL:KXN85817.1};
GN   ORFNames=AN958_10807 {ECO:0000313|EMBL:KXN85817.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN85817.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN85817.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN85817.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; KQ962426; KXN85817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QEY7; -.
DR   STRING; 1714833.A0A137QEY7; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 4.
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; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR   PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR   PANTHER; PTHR31273:SF1; PHOSPHOKETOLASE-RELATED; 1.
DR   Pfam; PF03894; XFP; 2.
DR   Pfam; PF09363; XFP_C; 1.
DR   Pfam; PF09364; XFP_N; 2.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT   DOMAIN          1..87
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          88..241
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          431..634
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   659 AA;  73650 MW;  008C7FA69AD69993 CRC64;
     MLYVIGPGHG APGVLACLWL EDSLSTFWPK YSRNYEGLFN LITTFSIPGG FPSHINAQTP
     GAIHEVGELG YALSVAFGAA MDNPDLIYID PVETGAVLPI LHINGFKVSE RTTYGAMDDR
     KLVSFFVGYG YQPRMVEDME NIDRNLAASL SWAISEIHKI QHATRSGNPI IKPRWPVILL
     RTPGNIIEGS FQSHQVPLPK AKSDERHLRP LDAWLKSYNP RGLFQEDALP VKAVRKLIPS
     LGRKRESYKA YVPLDVPDWR LLAVRKVTQE RCMKRVGKFL GEAIASNSKT LRIFSPDGLV
     SNKLDAVLER TSRNFQWDTF STGRTGLFPS YKASLGIIHT VMVQYSKFMK LAQETQRRQP
     CGSLNYIETS NWTRQEHNGF SHQNPSFIGA VLNLRPEAAR VYLPPDANCA LSTVAHCIGA
     NNYVNLIVGS KQPTPVWLSR EETDKHCIAG ASVRKFASVD DDINPDVVLV GKGVEVTFEV
     IAAASLLCKH CLNLHVRAVN IIDLIVLNHK CTHPHALDDE QFNMLFTEDR PVHFNYHSYP
     IELQGLLFGR PGLMERVTIA GYKGEGTTTS PFDMMLCNNT SRFDFAIAAI RGGSRVNPKV
     AVNAHIEISA LRHEAKKVQD YIYKHGEDPE GTYTIVLLKH ILRYEGLFSI SLGVWLLSF
//