ID   A0A0D2IVD8_9EURO        Unreviewed;       811 AA.
AC   A0A0D2IVD8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Phosphoketolase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z518_09735 {ECO:0000313|EMBL:KIX00670.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX00670.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX00670.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX00670.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847482; KIX00670.1; -; Genomic_DNA.
DR   RefSeq; XP_013267806.1; XM_013412352.1.
DR   AlphaFoldDB; A0A0D2IVD8; -.
DR   STRING; 1442369.A0A0D2IVD8; -.
DR   GeneID; 25297806; -.
DR   VEuPathDB; FungiDB:Z518_09735; -.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000053617; 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:UP000053617};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          29..390
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          608..809
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   811 AA;  91374 MW;  DE155BB1A72EDC12 CRC64;
     MAPAADADLS VESISPFGKA RSTVKDTVLS EAELKLIDDY MRASLYLCLG MLYLRKNPLL
     KEPLKVEHLK ARLLGHWGSD AGQVFAYVHF NRLIKKYDID SIFISGPGHG APAVISQSYL
     EGVYSEVYPD KSEDVEGMRR FFKQFSFPGG IGSHATPETP GSLHEGGELG YSISHAFGAV
     FDHPDLIALT MVGDGESETG PLATSWHSTK FLNPITDGAV LPVLHLNGYK INNPTILARV
     SHKELEALFV GYGWTPYFVE GSDPMSMHHA MAATLEKCVV EIRAHQKKAR ESGKAFRPLW
     PMVILRSPKG WTGPRTVDGH YLEGFWRSHQ IPLPDVASSP EHLKVLEDWM KSYTPEKYFT
     EDGKLIPELK ALVPEGNRRM SANPVANGGL LKKHLHMPDF RDYKIEVKRG GTTEAPSMSN
     MAIFLRDIIE KNQTNFRLFG PDETESNKLG AVYKAGKKVW MGEYFDEDAD GGNLAFEGRV
     MEMLSEHTVE GWLEGYVLSG RHGLLNSYEP FIHIIDSMVN QHCKWIEKCL EVEWRSKIAS
     LNILLTATVW RQDHNGFTHQ DPGFLDVVAN KSPEVVRIYL PPDGNCLLSC MDHCLRSSNY
     VNVIVADKQN HLQYLDMEAA IEHCTKGAGI WDWASNDQGQ EPDVVMASCG DVPTMESLAA
     TALLREYIPE LKIRFVNVVD LFRIIPHGEH PHGMTDREFT AIFTDDKPVI FNFHSYPWLI
     HRLTYRRKGQ HNLHVRGYNE KGNIDTPLEL AIRNQTDRFS LAIDALDRMP ALGNKGASAR
     EKLLNEQIKC RNEAFHEGID PEAIRKWVWP F
//