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
//