ID   XPKA_LACPE              Reviewed;         788 AA.
AC   Q937F6;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   28-JUN-2023, entry version 61.
DE   RecName: Full=Xylulose-5-phosphate phosphoketolase;
DE            EC=4.1.2.9;
GN   Name=xpkA;
OS   Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-32; 478-489 AND
RP   651-659, AND FUNCTION.
RC   STRAIN=MD363;
RX   PubMed=11823225; DOI=10.1128/aem.68.2.831-837.2002;
RA   Posthuma C.C., Bader R., Engelmann R., Postma P.W., Hengstenberg W.,
RA   Pouwels P.H.;
RT   "Expression of the xylulose 5-phosphate phosphoketolase gene, xpkA, from
RT   Lactobacillus pentosus MD363 is induced by sugars that are fermented via
RT   the phosphoketolase pathway and is repressed by glucose mediated by CcpA
RT   and the mannose phosphoenolpyruvate phosphotransferase system.";
RL   Appl. Environ. Microbiol. 68:831-837(2002).
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000305};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC   -!- INDUCTION: Induced by sugars that are fermented by the phosphoketolase
CC       pathway (PKP) and repressed by glucose mediated by carbon catabolite
CC       protein A and by the mannose phosphoenolpyruvate phosphotransferase
CC       system.
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ309011; CAC84393.1; -; Genomic_DNA.
DR   RefSeq; WP_050339622.1; NZ_RIOZ01000047.1.
DR   AlphaFoldDB; Q937F6; -.
DR   SMR; Q937F6; -.
DR   STRING; 1589.GCA_001188985_02619; -.
DR   GeneID; 49394776; -.
DR   OrthoDB; 9768449at2; -.
DR   BRENDA; 4.1.2.9; 2886.
DR   GO; GO:0050193; F:phosphoketolase activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Thiamine pyrophosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11823225"
FT   CHAIN           2..788
FT                   /note="Xylulose-5-phosphate phosphoketolase"
FT                   /id="PRO_0000193868"
SQ   SEQUENCE   788 AA;  88705 MW;  C9AE9E7819CF8753 CRC64;
     MSTDYSSPAY LQKVDKYWRA ANYLSVGQLY LKDNPLLQRP LKASDVKVHP IGHWGTIAGQ
     NFIYAHLNRV INKYGLKMFY VEGPGHGGQV MVSNSYLDGT YTDIYPEITQ DVEGMQKLFK
     QFSFPGGVAS HAAPETPGSI HEGGELGYSI SHGVGAILDN PDEIAAVVVG DGESETGPLA
     TSWQSTKFIN PINDGAVLPI LNLNGFKISN PTIFGRTSDE KIKQYFESMN WEPIFVEGDD
     PEKVHPALAK AMDEAVEKIK AIQKNAREND DATLPVWPMI VFRAPKGWTG PKSWDGDKIE
     GSFRAHQIPI PVDQTDMEHA DALVDWLESY QPKELFNEDG SLKDDIKEII PTGDARMAAN
     PITNGGVDPK ALNLPNFRDY AVDTSKHGAN VKQDMIVWSD YLRDVIKKNP DNFRLFGPDE
     TMSNRLYGVF ETTNRQWMED IHPDSDQYEA PAGRVLDAQL SEHQAEGWLE GYVLTGRHGL
     FASYEAFLRV VDSMLTQHFK WLRKANELDW RKKYPSLNII AASTVFQQDH NGYTHQDPGA
     LTHLAEKKPE YIREYLPADA NSLLAVGDVI FRSQEKINYV VTSKHPRQQW FSIEEAKQLV
     DNGLGIIDWA STDQGSEPDI VFAAAGTEPT LETLAAIQLL HDSFPDMKIR FVNVVDILKL
     RSPEKDPRGL SDAEFDHYFT KDKPVVFAFH GYEDLVRDIF FDRHNHNLHV HGYRENGDIT
     TPFDVRVMNQ MDRFDLAKSA IAAQPAMENT GAAFVQDMDN MLAKHNAYIR DAGTDLPEVN
     DWQWKGLK
//