ID   A0A0G2G1S6_9EURO        Unreviewed;       816 AA.
AC   A0A0G2G1S6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=Putative xylulose-5-phosphate phosphoketolase {ECO:0000313|EMBL:KKY17843.1};
GN   ORFNames=UCRPC4_g05308 {ECO:0000313|EMBL:KKY17843.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY17843.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY17843.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY17843.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY17843.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY17843.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-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:KKY17843.1}.
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DR   EMBL; LCWF01000136; KKY17843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2G1S6; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000053317; 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   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          35..395
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          613..814
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   816 AA;  91705 MW;  A2EB07E623C98903 CRC64;
     MAAPAKSTET DGEVQVKSIS PYGTARSTAS GEPLTAEEIR LYNEYFQASL YLCLGMLYLQ
     KNPLLKEKLD PSHIKPRSLG HWGSDAGQIF TYMHFNRLIK KYDLDAIFIS GPGHGAPAVL
     SQAYLEGTYS EVYPDKSEDS EGLQRFFKQF SFPGGVGSHA TPETPGSLHE GGELGYSISH
     AFGTVYDNPD LISVTMVGDG ESETGPLAAS WHSTKFLNPI TDGAVLPVLH LNGYKINNPT
     VLARISHEEL EALFVGYGWT PYFVEGSDVE SMHQAMAATF EKCVTEIKAV QKKARESKKA
     FRPRWPMIIL RSPKGWTGPR KVDSHYLEGF WRSHQIPLPD ARTNPEHLLV LESWMKSYQP
     EIVFDATGKL KPELKALTPE GNKRMSANPV ANGGILRKPL RMPDFRSFAV DVRKAGVTEF
     GSMAQLGKFF RDIIKSNPTN FRAFGPDETE SNKLGAMYEA GKKVWLGDYF AEDEDGGNLA
     FAGRVMEILS EHTVEGWLEG YLLSGRHGFL NSYEPFIHII DSMVNQHCKW IEKCNEVEWR
     VKIASLNILL TATVWRQDHN GFTHQDPGFL DVVANKSPEV VRIYLPPDGN CLLSTADHCL
     RSTNYVNVIV ADKQNHLQYL DMEAAVEHCT KGAGIWKWAS NDDGFEPDVV MASCGDVPTH
     ESLAATALLR EYVPDIKIRF VNVVDLFKLI AEKEHSHGLS DVEYSALFTY DKPVIFNFHS
     YPWLIHRLTY QRKGQSNMYV TGYREKGNIN TPLELAIRNG TDRFSLAIAA IDRVPRLHNT
     ASAVRESFLN EQIAARNHAW EFGIDDKKYT EWKWPY
//