ID   T1B4H4_9ZZZZ            Unreviewed;       384 AA.
AC   T1B4H4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   SubName: Full=Phosphate/d-fructose 6-phosphate phosphoketolase {ECO:0000313|EMBL:EQD67861.1};
DE   Flags: Fragment;
GN   ORFNames=B1B_05785 {ECO:0000313|EMBL:EQD67861.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD67861.1};
RN   [1] {ECO:0000313|EMBL:EQD67861.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD67861.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
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:EQD67861.1}.
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DR   EMBL; AUZY01003671; EQD67861.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1B4H4; -.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02011; TPP_PK; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
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; PF09364; XFP_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   4: Predicted;
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          35..384
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         384
FT                   /evidence="ECO:0000313|EMBL:EQD67861.1"
SQ   SEQUENCE   384 AA;  41673 MW;  0104754962321BAC CRC64;
     MDGPRYGGEP TLPPAGAGQG HAVSASAADP GRPLREDEVA RIDAYWRAAN YLSVGQIYLM
     DNPLLRQPLR PDQVKPRLLG HWGTTPGINF VYAHMNRVIR NWDLNALLVI GPGHGGPAAV
     ANAYLEGTYT EVYPLISWNE DGLRRLFRQF SFPGGIPSHV APETPGSINE GGELGYSLAH
     AYGAAFDNPE LLVCCIVGDG EAETGALATG WHSNKFLNPA TDGAVLPILH LNGYKIANPT
     VLARIGDGEL TSLLEGYGYA VHWVSGDVPA EMHRAMADTL DSAVGEILRI QRAARSGSTG
     QRPRWPLIVL RTPKGWTGPK MVDGLPVEGT WRAHQVPLPE VRTNPEHLAQ LEAWMRSYRP
     EELFDAEGAF LPELASLAPK GQRR
//