ID PHK_BIFA0 Reviewed; 825 AA.
AC B8DUT6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Probable phosphoketolase {ECO:0000255|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_01403};
GN OrderedLocusNames=BLA_1483;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01403};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000255|HAMAP-
CC Rule:MF_01403}.
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DR EMBL; CP001213; ACL29765.1; -; Genomic_DNA.
DR RefSeq; WP_004217768.1; NC_011835.1.
DR AlphaFoldDB; B8DUT6; -.
DR SMR; B8DUT6; -.
DR STRING; 442563.BLA_1483; -.
DR GeneID; 66533313; -.
DR KEGG; bla:BLA_1483; -.
DR HOGENOM; CLU_013954_2_0_11; -.
DR Proteomes; UP000002456; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
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 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 3: Inferred from homology;
KW Lyase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..825
FT /note="Probable phosphoketolase"
FT /id="PRO_1000184576"
SQ SEQUENCE 825 AA; 92502 MW; 0E1D963806C61797 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 WITLDEARAE LEAGAAEWKW ASNAKSNDEV QVVLAAAGDV PTQEIMAASD
ALNKMGIKFK VVNVVDLIKL QSSKENDEAM SDEDFADLFT ADKPVLFAYH SYAQDVRGLI
YDRPNHDNFT VVGYKEQGST TTPFDMVRVN DMDRYALQAK ALELIDADKY ADKINELNEF
RKTAFQFAVD NGYDIPEFTD WVYPDVKVDE TSMLSATAAT AGDNE
//
