ID   XFP_BIFAS               Reviewed;         825 AA.
AC   Q9AEM9; C6AIU2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase;
DE            EC=4.1.2.22;
DE            EC=4.1.2.9;
GN   Name=xfp; OrderedLocusNames=Balat_0971;
OS   Bifidobacterium animalis subsp. lactis (strain DSM 10140 / JCM 10602 / LMG
OS   18314).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=555970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-31, AND
RP   CHARACTERIZATION.
RX   PubMed=11292814; DOI=10.1128/jb.183.9.2929-2936.2001;
RA   Meile L., Rohr L.M., Geissmann T.A., Herensperger M., Teuber M.;
RT   "Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate
RT   phosphoketolase gene (xfp) from Bifidobacterium lactis.";
RL   J. Bacteriol. 183:2929-2936(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10140 / JCM 10602 / LMG 18314;
RX   PubMed=19376856; DOI=10.1128/jb.00155-09;
RA   Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M.,
RA   Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L.,
RA   Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A.,
RA   Roberts R.F.;
RT   "Comparison of the complete genome sequences of Bifidobacterium animalis
RT   subsp. lactis DSM 10140 and Bl-04.";
RL   J. Bacteriol. 191:4144-4151(2009).
CC   -!- FUNCTION: Phosphoketolase using both fructose 6-phosphate and xylulose
CC       5-phosphate as substrate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-
CC         glyceraldehyde 3-phosphate + H2O; Xref=Rhea:RHEA:10468,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57737, ChEBI:CHEBI:59776; EC=4.1.2.9;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=keto-D-fructose 6-phosphate + phosphate = acetyl phosphate +
CC         D-erythrose 4-phosphate + H2O; Xref=Rhea:RHEA:12196,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:22191,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57579; EC=4.1.2.22;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000305};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10 mM for fructose 6-phosphate;
CC         KM=45 mM for xylulose 5-phosphate;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000305}.
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DR   EMBL; AJ293946; CAC29121.1; -; Genomic_DNA.
DR   EMBL; CP001606; ACS47899.1; -; Genomic_DNA.
DR   RefSeq; WP_012754421.1; NC_012815.1.
DR   AlphaFoldDB; Q9AEM9; -.
DR   SMR; Q9AEM9; -.
DR   KEGG; blt:Balat_0971; -.
DR   HOGENOM; CLU_013954_2_0_11; -.
DR   BioCyc; BANI555970:G1GVE-989-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-12656; -.
DR   BRENDA; 4.1.2.22; 6813.
DR   BRENDA; 4.1.2.9; 6813.
DR   GO; GO:0047905; F:fructose-6-phosphate phosphoketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0050193; F:phosphoketolase activity; IEA:UniProtKB-EC.
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   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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Thiamine pyrophosphate.
FT   CHAIN           1..825
FT                   /note="Xylulose-5-phosphate/fructose-6-phosphate
FT                   phosphoketolase"
FT                   /id="PRO_0000193867"
FT   CONFLICT        18
FT                   /note="S -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="E -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   825 AA;  92530 MW;  F1A418B84E7F97DF CRC64;
     MTNPVIGTPW QKLDRPVSEE AIEGMDKYWR VANYMSIGQI YLRSNPLMKE PFTRDDVKHR
     LVGHWGTTPG LNFLLAHINR LIADHQQNTV FIMGPGHGGP AGTAQSYIDG TYTEYYPNIT
     KDEAGLQKFF RQFSYPGGIP SHFAPETPGS IHEGGELGYA LSHAYGAIMD NPSLFVPCII
     GDGEAETGPL ATGWQSNKLV NPRTDGIVLP ILHLNGYKIA NPTILARISD EELHDFFRGM
     GYHPYEFVAG FDNEDHLSIH RRFAELFETI FDEICDIKAA AQTDDMTRPF YPMLIFRTPK
     GWTCPKFIDG KKTEGSWRAH QVPLASARDT EAHFEVLKGW MESYKPEELF NADGSIKEDV
     TAFMPKGELR IGANPNANGG RIREDLKLPE LDQYEITGVK EYGHGWGQVE APRSLGAYCR
     DIIKNNPDSF RVFGPDETAS NRLNATYEVT KKQWDNGYLS ALVDENMAVT GQVVEQLSEH
     QCEGFLEAYL LTGRHGIWSS YESFVHVIDS MLNQHAKWLE ATVREIPWRK PISSVNLLVS
     SHVWRQDHNG FSHQDPGVTS VLLNKTFNND HVTNIYFATD ANMLLAIAEK CFKSTNKINA
     IFAGKQPAAT WITLDEVRAE LEAGAAEWKW ASNAKSNDEV QVVLAAAGDV PTQEIMAASD
     ALNKMGIKFK VVNVVDLIKL QSSKENDEAM SDEDFADLFT ADKPVLFAYH SYAQDVRGLI
     YDRPNHDNFT VVGYKEQGST TTPFDMVRVN DMDRYALQAK ALELIDADKY ADKINELNEF
     RKTAFQFAVD NGYDIPEFTD WVYPDVKVDE TSMLSATAAT AGDNE
//