ID   B6Q4Z3_TALMQ            Unreviewed;       817 AA.
AC   B6Q4Z3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   13-SEP-2023, entry version 56.
DE   SubName: Full=Phosphoketolase, putative {ECO:0000313|EMBL:EEA27336.1};
GN   ORFNames=PMAA_022200 {ECO:0000313|EMBL:EEA27336.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA27336.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; DS995899; EEA27336.1; -; Genomic_DNA.
DR   RefSeq; XP_002143851.1; XM_002143815.1.
DR   AlphaFoldDB; B6Q4Z3; -.
DR   STRING; 441960.B6Q4Z3; -.
DR   VEuPathDB; FungiDB:PMAA_022200; -.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   OrthoDB; 5485390at2759; -.
DR   PhylomeDB; B6Q4Z3; -.
DR   Proteomes; UP000001294; 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:UP000001294};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          30..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   817 AA;  91719 MW;  16CFF81D1C869C0E CRC64;
     MAPGAIDVNI QSISAYGPAR STVKVDKPLS SDEVHKINEY FKASLYLCLG MLYLRDNPLL
     KEPLKKEHIK NRVLGHWGSD AGQSFTWIHM NRLIKKYSLD SLFISGPGHG APGILSQSYL
     EGVYSEVYPD KTEDEDGMRR FFKSFSFPGG IGSHATPETP GSIHEGGELG YSISHAFGAV
     YDHPDLIALT MVGDGEAETG PLATSWHSTK FLNPITDGAV LPVLHLNGYK INNPTLLARI
     SHEELEALFI GYGWAPYFVE GSDLQSMHQS MAATLEHCVL DIKEIQKKAR ESKKAFRPRW
     PMIVLRTPKG WTAPREVDGK RLEGFWRSHQ VPMPDVLTNP DHLKLLESWM KSYGPDELFA
     NKGKLIPELK ALAPTGNSRM SANPVGNGGL LRKPLDLPDF RTYGVQKIEP GVSLIGNMTN
     LAKFLRDVIA KNKTNFRLFG PDETESNKLG EVYKAGKKVW LGAYFDEDQD GGNLAMEGRV
     MEMLSEHTIE GWLEGYILSG RHGLLNSYEP FIHIIDSMVN QHCKWLEKCL EVEWRAKVAS
     LNILLTATVW RQDHNGFTHQ DPGFLDVVAN KSPEVVRIYL PPDGNSLLSV ADHCLRSVNY
     VNVIVADKQE HLQFLSMEEA IEHCTKGVGI WDWASNDQGE EPDVVMASAG DVATHEALAA
     TALLRQYLPG VKVRFVNVVD LFRLIPETQH PHGMSDLQWK ALFTEDKPII FNFHSYPFLV
     HRLTYRRPGQ KNLHVRGYRE KGNIDTPFEL AVRNETDRFS LAIAAIDNIP RLHNTASAIR
     EKFVNSQIAA RNTAFGDGVD SEEIRTWKWP FPKKELI
//