ID   PHK_THEVB               Reviewed;         812 AA.
AC   Q8DJN6;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable phosphoketolase {ECO:0000255|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_01403};
GN   OrderedLocusNames=tll1186;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01403};
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01403}.
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DR   EMBL; BA000039; BAC08738.1; -; Genomic_DNA.
DR   RefSeq; NP_681976.1; NC_004113.1.
DR   RefSeq; WP_011057028.1; NC_004113.1.
DR   AlphaFoldDB; Q8DJN6; -.
DR   SMR; Q8DJN6; -.
DR   STRING; 197221.22294910; -.
DR   EnsemblBacteria; BAC08738; BAC08738; BAC08738.
DR   KEGG; tel:tll1186; -.
DR   PATRIC; fig|197221.4.peg.1247; -.
DR   eggNOG; COG3957; Bacteria.
DR   OMA; LSTMDHC; -.
DR   OrthoDB; 45239at2; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
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; PTHR31273; 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; SSF52518; 2.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..812
FT                   /note="Probable phosphoketolase"
FT                   /id="PRO_0000193892"
SQ   SEQUENCE   812 AA;  91579 MW;  C0BE01C19D4DF75F CRC64;
     MVSSPPRPTA LTDDIHAFGP ARATIQGQPL SDSEVEAMDA FFRACNYLAV GMIYLLDNPL
     LKEPLKPEHI KKRLLGHWGS SPGLAFCYLH LNRIIKKYQQ EVIFLAGPGH GAPGVLAPVY
     LEGSYSEIYP NISEDAAGLK KFFKQFSFPG GIGSHCTPET PGSIHEGGEL GYVLSHACGA
     AFDNPDLIVA AVVGDGEAET APLATSWHIN KFLNPARDGA VLPILNLNGY KINNPTILAR
     IPHQDLENYF RGLGYDPCFV EGSDRPSMHQ AMAATLDYCV TRIKEIQRTA REEGLTTLPR
     WPMIVLRTPK GWTGPAEVNG HKVEGSWRAH QVPLADVHTN PENLQLLENW LRSYRPEELF
     DHNGTFRPDL KALAPTGNYR MGMNPHANGG LLRKDLKMPN FREYGITFDK PGQIEVENTR
     PLGVFLRDVM RNNPRNFRIF GPDETTSNKL NAVYEASKKF WIAESFDEDA DGGELSPEGR
     VIEMLSEHTL EGMLEGYLLT GRHGFFSTYE AFVHVIDSMF NQHAKWLSIC NELSWRADVS
     SLNLLITSTV WRQDHNGFTH QDPGFLDIVC NKSAKVTRIY LPPDVNSLLS VADHCLRSKN
     YVNVIVSDKQ LHLQYLTMDQ AIIHCTKGVG IWDWASNDQG YEPDLVMASA GDIPTQEALA
     AIALLRQEFP ELKIRYINVV DLFKLQPETE HPHGLSDRDF DSLFTLDRPI IFNFHGYPWL
     IHRLAYRRHN HRNLHVRGYK EKGNINTPLE LAINNEIDRF SLAIDAIDRL PELQVAGAHA
     KEKFRNMQIA ARNYAYEYGV DKPEFSHWTW PF