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Database: UniProt
Entry: A0A086ZVF6_9BIFI
LinkDB: A0A086ZVF6_9BIFI
Original site: A0A086ZVF6_9BIFI 
ID   A0A086ZVF6_9BIFI        Unreviewed;       825 AA.
AC   A0A086ZVF6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:KFI50506.1};
DE            EC=4.1.2.22 {ECO:0000313|EMBL:KFI50506.1};
DE            EC=4.1.2.9 {ECO:0000313|EMBL:KFI50506.1};
GN   ORFNames=BBIA_1729 {ECO:0000313|EMBL:KFI50506.1};
OS   Bifidobacterium biavatii DSM 23969.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI50506.1, ECO:0000313|Proteomes:UP000029108};
RN   [1] {ECO:0000313|EMBL:KFI50506.1, ECO:0000313|Proteomes:UP000029108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI50506.1,
RC   ECO:0000313|Proteomes:UP000029108};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI50506.1}.
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DR   EMBL; JGYN01000015; KFI50506.1; -; Genomic_DNA.
DR   RefSeq; WP_033495618.1; NZ_JGYN01000015.1.
DR   AlphaFoldDB; A0A086ZVF6; -.
DR   STRING; 1437608.GCA_000771645_01414; -.
DR   eggNOG; COG3957; Bacteria.
DR   OrthoDB; 9768449at2; -.
DR   Proteomes; UP000029108; Unassembled WGS sequence.
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: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   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   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
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:KFI50506.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029108};
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;  92458 MW;  186462CF56AFEAD1 CRC64;
     MTSPVIGTPW KKLNAPVSEE SLEGVDKYWR AANYLSIGQI YLRSNPLMKA PFTREDVKHR
     LVGHWGTTPG LNFLIGHINR FIADHSQNTV IIMGPGHGGP AGTSQSYLDG TYTETFPKIT
     KDEAGLQKFF RQFSYPGGIP SHFAPETPGS IHEGGELGYA LSHAYGAIMN NPSLFVPAIV
     GDGEAETGPL ATGWQSNKLV NPRTDGIVLP ILHLNGYKIA NPTILSRISD EELHEFFHGM
     GYEPYEFVAG FDDEDHMSIH RRFAELFENV WDEICDIKAA AQTDDVHRPF YPMIIFRTPK
     GWTCPKFIDG KKTEGSWRSH QVPLASARDT EAHFEVLKNW LESYKPEELF DEKGAIRPEV
     TAFMPKGELR IGANPNANGG LIREDLKLPK LEDYEVKEVQ EYGHGWGQLE ATRRLGVYTR
     DIIKLNPDSF RIFGPDETAS NRLQAAYDVT NKQWDAGYLS EQVDEHMAVT GQVTEQLSEH
     QMEGFLEAYL LTGRHGIWSS YESFVHVIDS MLNQHAKWLE ATVREIPWRK PISSMNLLVS
     SHVWRQDHNG FSHQDPGVTS VLLNKCFNND HVIGIYFPVD SNMLLAVAEK CYKSTNKINA
     IIAGKQPAAT WLTLDEARAE LEKGAAEWKW ASNVESNDEA DIVLAAAGDV PQQELMAAAD
     KLAALGIKFK VVNVVDLLAL QSAKENDEAL SDEEFAEIFT ADKPVLFAYH SYARDVRGLI
     YDRPNHDNFN VHGYEEQGST TTPYDMVRVN NIDRYELTAE ALRMVDAEKF ADKINELEAF
     RQEAFQFAVD NGYDHPDYTD WVYSGVKTDV QGAVTATAAT AGDNE
//
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