ID   W6PW81_PENRF            Unreviewed;       819 AA.
AC   W6PW81;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   SubName: Full=Probable phosphoketolase 1 {ECO:0000313|EMBL:CDM28041.1};
GN   ORFNames=PROQFM164_S01g001852 {ECO:0000313|EMBL:CDM28041.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM28041.1};
RN   [1] {ECO:0000313|EMBL:CDM28041.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM28041.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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; HG792015; CDM28041.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6PW81; -.
DR   STRING; 1365484.W6PW81; -.
DR   OMA; TMDHCLR; -.
DR   OrthoDB; 5485390at2759; -.
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          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   819 AA;  92088 MW;  E353C003F9E0B67B CRC64;
     MSGSAVVHSM TPIPDEMSIS AYGEARSTVE GKPLDAETIR KMNAWFRASM YLCLGMLYLR
     DNPLLEEPLK LEHLKARLLG HWGSDAGQAF TWMHMNRLIK KYDLDVLFVS GPGHGAPAIL
     SQSYLEGVYS EVYPEKGQDK QGMQKFFKQF SFPGGIGSHA TPETPGSIHE GGELGYSLSH
     AFGTVYDHPN LITLTMVGDG ESETGPLATS WHSTKFLNPI NDGAVLPVLH LNGYKINNPT
     VLARISHSEL SSLLVGYGWK PYFVEGSDFD SMHQAMAATL EQCVTEIRGY QKKARDSKVP
     FRPRWPMIIL RTPKGWSAPR EVDGHLLEGF WRAHQIPITD VRENPAHLKV LETWMRGYKP
     EELFDKNGTL IPELRELAPT GTSRISANPV GNGGLLRRPL DIPDFRDYGF NDIVPGITTK
     GGMANMAKFL RDIVARNMHN FRLFGPDETE SNKLAEVYKA GKKVWMGDYF EEDKDGGNLS
     PDGRVMEILS EHTCEGWLEG YILSGRHGLL NSYEPFIHVI DSMVNQHCKW IEKSLEIEWR
     ARVSSLNILI TATVWRQDHN GFSHQDPGFL DVVANKSPEV VRIYLPPDGN TLLSVMDHCL
     RSVNYVNVVV ADKQEHIQFL NMDEALAHCT KGLGIWDWAS NDQGQDPDVV MASCGDVSTY
     EALAATALLR EHLPQLKVRF VNVVDLFRLI SPVNHPHGLS DARWKSIFTN DTPIIFNFHS
     YPWLIHRLTY KRVGQHNLHV RGYKEKGNID TPFELAVRNG TDRYSLAMAA IDSVQSLGNT
     ADGVREKLLN EQIAGRSEAL DNGIDAEHIR NWKWPFPRE
//