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Database: UniProt
Entry: A0A137QVA6_9AGAR
LinkDB: A0A137QVA6_9AGAR
Original site: A0A137QVA6_9AGAR 
ID   A0A137QVA6_9AGAR        Unreviewed;       483 AA.
AC   A0A137QVA6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative phosphoketolase {ECO:0000313|EMBL:KXN91188.1};
GN   ORFNames=AN958_02641 {ECO:0000313|EMBL:KXN91188.1};
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:KXN91188.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN91188.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN91188.1,
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; KQ962012; KXN91188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QVA6; -.
DR   STRING; 1714833.A0A137QVA6; -.
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; -; 2.
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; PF09363; XFP_C; 1.
DR   Pfam; PF09364; XFP_N; 2.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT   DOMAIN          45..137
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          138..216
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          255..457
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  53451 MW;  7FD23AFEF83AF61D CRC64;
     MPGQQLTQPN LPPNPSHIPD SISPQVVQLE YTKFLNRDDL TSIRSFRRAA DYIAAGPGHG
     APGVLACLWL EDSLSTFWPK YSRNYEGLFN LITTFSIPGG FPSHINAQTP GAIHEVGELG
     YALSVAFGAA MDNPDLIYID PVETGAVLPI LHINGFKVSE RTTYGAMDDR ELVSFFIGYG
     YQPRMVKDME NIDHDLAALL SWAISKIHKI QHAALLNLKP EAARVYLPPD ANCALSTVAH
     CIGVNNYVNL IIGSKQPMLV WLSCEETDKH CIAGASVRKF ASVDDNINSN VILVGKGVEV
     TFEVIAAMSL LCKHCLNLHI RAVNVIDLIV LNHKWAHPHA LDDEQFNMLF TEDRPIHFNY
     HGYPIELQGL LFGHPGLMER VTIAGYKGEG MTTSPFDMML CNNTSRFDFA IAAICGGSRV
     NPKVAVNAHI EISALRHEAK KVQDYIYKHG EDPEGTYTII LLKHILCYEG LFSISLGVWL
     LSF
//
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