ID   A0A093Y8I0_9PEZI        Unreviewed;       811 AA.
AC   A0A093Y8I0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=O988_02850 {ECO:0000313|EMBL:KFY01239.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY01239.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFY01239.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY01239.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY01239.1}.
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DR   EMBL; JPJR01000454; KFY01239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Y8I0; -.
DR   STRING; 1391699.A0A093Y8I0; -.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   Proteomes; UP000029329; 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:UP000029329};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          30..389
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          607..809
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   811 AA;  91369 MW;  3724BC94A76E2F4D CRC64;
     MATPAETDIT VKSISPYGKA RSTVQGAPLA PDELKKMDDY MRASLYLCLG MIHLKQNPLL
     KEPLKVDHLK ARLLGHWGSD SGQIFTYIHA NRMIKKYDLD AFFISGPGHG APAVLSQAYL
     EGTYSEVYPD KSEDEDGMQR FFKQFSFPGG IGSHATPETP GSIHEGGELG YSISHAFGSV
     FDHPNLIAVT MVGDGESETG PLATSWHSTK FLNPIVDGAV LPVLHLNGYK INNPTILARV
     SHRELEALFI GYGWQPYFVE GSDHETMHQA MAATVEKCIT EIRGYQKKAR DSGKPFRPFW
     PMIILRTPKG WTAPRDIDGH FLEGFWRAHQ IPIPDIAKNK EHFKIFEKWM RSYEPERLFQ
     DGKLIPELRE LPPKGNSRMS ANPVANGGIL RKPLHVPDFR DYAIDVPRNG HALGPSMENM
     AIFLRDIISK NQTNFRVFGP DETQSNKLDG IYAAGKKVWM AETFEEDADG GNLAFAGRVM
     EMLSEHTVEG WLEGYILSGR HGLLNSYEPF IHIIDSMVNQ HCKWIEKSLE TSWRVKIASL
     NILLTATVWR QDHNGFTHQD PGFLAVVAQK SPEVVRIYLP PDGNCLLSVM DHCFRSENYV
     NVVVADKQEH LQFLSMEDAV VHCTKGIGIW EWASNDKDAD PDVVMASCGD ISTQEALAAV
     ALLRQHLPDL KVRFVNVVDL FKLISAADHP HGLSDSAYSS IFTADKPIIF NFHSYPFLIH
     RLTYKRPGST NMHVRGYREK GNIDTPLELA IRNQTDRYSL AMDALQRLEG QLHNRGAATR
     EALLEEQIKM RNWAFEHGTD PDEITNWVWP Y
//