ID Q6R2R0_BIFAD Unreviewed; 825 AA.
AC Q6R2R0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 28-JUN-2023, entry version 50.
DE SubName: Full=Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase {ECO:0000313|EMBL:AAR98784.1};
DE EC=4.1.2.22 {ECO:0000313|EMBL:AAR98784.1};
GN Name=xfp {ECO:0000313|EMBL:AAR98784.1};
OS Bifidobacterium adolescentis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1680 {ECO:0000313|EMBL:AAR98784.1};
RN [1] {ECO:0000313|EMBL:AAR98784.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFAR 335 {ECO:0000313|EMBL:AAR98784.1};
RX PubMed=15899413; DOI=10.1016/j.femsle.2005.04.013;
RA Yin X., Chambers J.R., Barlow K., Park A.S., Wheatcroft R.;
RT "The gene encoding xylulose-5-phosphate/fructose-6-phosphate
RT phosphoketolase (xfp) is conserved among Bifidobacterium species within a
RT more variable region of the genome and both are useful for strain
RT identification.";
RL FEMS Microbiol. Lett. 246:251-257(2005).
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 ---------------------------------------------------------------------------
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; AY518212; AAR98784.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6R2R0; -.
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: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; 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 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AAR98784.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 17..381
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 605..802
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 825 AA; 92560 MW; 2B3E3D62E60B1A09 CRC64;
MTSPVIGTPW KKLNAPVSEE AIEGVDKYWR AANYLSIGQI YLRSNPLMKE PFTREDVKHR
LVGHWGTTPG LNFLIGHINR LIADHQQNTV IIMGPGHGGP AGTAQSYLDG TYTEYFPNIT
KDEAGLQKFF RQFSYPGGIP SHYAPETPGS IHEGGELGYA LSHAYGAVMN NPSLFVPAIV
GDGEAETGPL ATGWQSNKLI NPRTDGIVLP ILHLNGYKIA NPTILSRISD EELHEFFHGM
GYEPYEFVAG FDNEDHLSIH RRFAELFETV FDEICDIKAA AQTDDMTRPF YPMIIFRTPK
GWTCPKFIDG KKTEGSWRSH QVPLASARDT EAHFEVLKNW LESYKPEELF DENGAVKPEV
TAFMPTGELR IGENPNANGG RIREELKLPK LEDYEVKEVA EYGHGWGQLE ATRRLGVYTR
DIIKNNPDSF RIFGPDETAS NRLQAAYDVT NKQWDAGYLS AQVDEHMAVT GQVTEQLSEH
QMEGFLEGYL LTGRHGIWSS YESFVHVIDS MLNQHAKWLE ATVREIPWRK PISSMNLLVS
SHVWRQDHNG FSHQDPGVTS VLLNKCFNND HVIGIYFPVD SNMLLAVAEK CYKSTNKINA
IIAGKQPAAT WLTLDEARAE LEKGAAEWKW ASNVKSNDEA QIVLAATGDV PTQEIMAAAD
KLGAMGIKFK VVNVVDLVKL QSAKENNEAL SDEEFAELFT EDKPVLFAYH SYARDVRGLI
YDRPNHDNFN VHGYEEQGST TTPYDMVRVN NIDRYELQAE ALRMIDADKY ADKINELEAF
RQEAFQFAVD NGYDHPDYTD WVYSGVNTNK QGAISATAAT AGDNE
//
