XPKA_LACPE
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 25-MAY-2022, entry version 57.
DE RecName: Full=Xylulose-5-phosphate phosphoketolase;
DE EC=4.1.2.9;
GN Name=xpkA;
OS Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC Bacteria; Firmicutes; 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}.
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DR EMBL; AJ309011; CAC84393.1; -; Genomic_DNA.
DR RefSeq; WP_050339622.1; NZ_PUFM01000036.1.
DR AlphaFoldDB; Q937F6; -.
DR SMR; Q937F6; -.
DR STRING; 1589.GCA_001188985_02619; -.
DR GeneID; 49394776; -.
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 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 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