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Database: UniProt
Entry: D4L332_9FIRM
LinkDB: D4L332_9FIRM
Original site: D4L332_9FIRM 
ID   D4L332_9FIRM            Unreviewed;       791 AA.
AC   D4L332;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   ORFNames=RO1_37910 {ECO:0000313|EMBL:CBL14022.1};
OS   Roseburia intestinalis XB6B4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=718255 {ECO:0000313|EMBL:CBL14022.1, ECO:0000313|Proteomes:UP000008953};
RN   [1] {ECO:0000313|EMBL:CBL14022.1, ECO:0000313|Proteomes:UP000008953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB6B4 {ECO:0000313|EMBL:CBL14022.1,
RC   ECO:0000313|Proteomes:UP000008953};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Roseburia intestinalis XB6B4.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL14022.1, ECO:0000313|Proteomes:UP000008953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB6B4 {ECO:0000313|EMBL:CBL14022.1,
RC   ECO:0000313|Proteomes:UP000008953};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|HAMAP-Rule:MF_01403};
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623,
CC       ECO:0000256|HAMAP-Rule:MF_01403}.
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DR   EMBL; FP929050; CBL14022.1; -; Genomic_DNA.
DR   RefSeq; WP_015522202.1; NC_021012.1.
DR   AlphaFoldDB; D4L332; -.
DR   GeneID; 61434619; -.
DR   KEGG; rix:RO1_37910; -.
DR   PATRIC; fig|718255.3.peg.1147; -.
DR   HOGENOM; CLU_013954_2_0_9; -.
DR   Proteomes; UP000008953; Chromosome.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02011; TPP_PK; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
FT   DOMAIN          12..371
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          589..789
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
FT   COILED          251..278
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   791 AA;  89895 MW;  F23359C3A55A5BED CRC64;
     MAEVNAVEKQ PVTQEYLKKM DAYWRAANYL GAAQLYLLDN PLLREPLTMD HIKKKIVGHW
     GTVPGQNFVY VHLNRVIKKY DQDMILISGP GHGGNFFVAN TYLEGTYSEV YPNIGEDMDG
     LKKLCKQFSF PGGISSHVAP ETPGSINEGG ELGYSLAHSF GAVFDNPDLV AACIVGDGES
     ETGPLATSWQ CNKFLNPKTD GAVLPILHLN GYKISNPTIL ARISREELEH FFDGCGWKPY
     FVEGDEPMDM HSKMAAALDQ AMDEIKAIQK NARENDDLTR PKWPMIVLRT PKGWTGPKVV
     DGNQIEGSFR AHQVPIMMDK PEHLQMLKDW LLSYHPEELF DEDGKLIPEL KALAPTGDRR
     IGSNPHANGG KLLRDLRLPD FKDYAVDVPK PGAVEAQDMI ELGGFVRDIF ELNEDAKNFR
     IFGPDETMSN RLGKVFEATN RDWNGEAYDT DEFLAHDGRV MDSMLSEHMC EGWLEGYLLT
     GRHGFFASYE AFIRVVDSMC AQHAKWLKVC NQLPWRQSIA SLNLILSSNV WQQDHNGFTH
     QDPGFLDHIA NKKSDVVRLY LPPDANCLLS CFDHCIRSRN YVNVLVTSKH PRQQWLTMEQ
     AVKHCTQGIG IWEWASNDQG EEPDVVMACC GDTPTLETLA AVTILREALP EIKIRVINVV
     DLMKLEPNTK HPHGLSDAEY DALFTKDKPI IFAFHGYHTL IHELTYRRTN RNIHVYGYQE
     EGTITTPFDM RVQNEIDRFH LVKNVIKYLP QLGNRGSYLV QQMNDKLVEH KQYIHEYGQD
     LPEVRDWKWN L
//
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