ID   A0A0N0SG07_9ACTN        Unreviewed;       682 AA.
AC   A0A0N0SG07;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:KOU43633.1};
GN   ORFNames=ADK54_17380 {ECO:0000313|EMBL:KOU43633.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU43633.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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}.
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:KOU43633.1}.
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DR   EMBL; LGDD01000212; KOU43633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0SG07; -.
DR   PATRIC; fig|1415557.3.peg.3860; -.
DR   Proteomes; UP000037774; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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; 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   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          4..328
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          526..675
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   682 AA;  71875 MW;  4366060A60D91741 CRC64;
     MAAWRALNYL CAAQLYVNDN VLPVRPLRVQ DVKEAPSGHW GVCPPVNFML AQLGPLTAGR
     PPGSEVLIVH GAGHAGPSAL AHAYLTKVLT LAGNQPGWSA AGLRALAAGF PHTRVYGEEI
     TPLIPGVRYT GGQLGPALAV AQGMVLDSPH RLVVALLGDG ELETGTAAAA WTARRALFGS
     GLHGVVLPVV LANGLRMGGP SLLAGLDEDE LRAYFTGLGY EPFRHDGSDV AGFRTVLAEV
     FARLRPLGAA RPQPVLVLTM PKGATGPEQV GGRRIAGTPA VHKTPLKDPA RNREEFDALA
     AWLSSYRPGE LFTERGQPCD LVRQALPHPA PRPRPAPPVA PLAVRGAEAW PLVSTVIRER
     AAAGSFRLFS PDEAASNRLR LAADGADDQL PEWAIEILNE EICHAWLQGY TETGRDALLA
     TYEAFAAVNT SLLVQHLKHR SARTATGTGG LANINYLITS LGWRNTYTHQ NPGLVSAMLE
     TENPTVHVYT PADATRAAAV LAVMLAGRDQ ANFLIADKHH PLTFPPDTFR EELTNGAAIW
     PHLSAPGSES PDIVLASAGD VAAREVSAAA GRLAAARPDA RIRYVHVNDL TVLGAPGTWP
     AALSDGTFAG LFPAGVPVLL ATVTQAPAVR ALLAGRGDAA RVHVVGYRDP GRPLPSADLL
     EQCGMSAAAL TAQALSMLKE PR
//