XFP_BIFAS
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 03-AUG-2022, entry version 98.
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; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC 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 AlphaFoldDB; Q9AEM9; -.
DR SMR; Q9AEM9; -.
DR PRIDE; Q9AEM9; -.
DR KEGG; blt:Balat_0971; -.
DR HOGENOM; CLU_013954_2_0_11; -.
DR OMA; LSTMDHC; -.
DR BioCyc; BANI555970:G1GVE-989-MON; -.
DR BioCyc; MetaCyc:MON-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: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 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