ID   Q2K4N7_RHIEC            Unreviewed;       795 AA.
AC   Q2K4N7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   OrderedLocusNames=RHE_CH03442 {ECO:0000313|EMBL:ABC92199.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC92199.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC92199.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC92199.1; -; Genomic_DNA.
DR   RefSeq; WP_011426668.1; NC_007761.1.
DR   AlphaFoldDB; Q2K4N7; -.
DR   KEGG; ret:RHE_CH03442; -.
DR   eggNOG; COG3957; Bacteria.
DR   HOGENOM; CLU_013954_2_0_5; -.
DR   OrthoDB; 9768449at2; -.
DR   Proteomes; UP000001936; 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   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
FT   DOMAIN          12..373
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          590..792
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   795 AA;  89698 MW;  9ADDECAD36CE4E40 CRC64;
     MEKHVSTAAA LTDVELTLID RYWRAANYLS VGQIYLLANP LLREPLKSEH IKPRLLGHWG
     TTPGLNFLYA HLNRVIRARD LDIIYICGPG HGGPGMVANT YLEGTYSEIY PDISEDTEGM
     RRLFRQFSFP GGIPSHAAPE TPGSIHEGGE LGYALVHAYG AAFDNPDLTV ACIVGDGEAE
     TGPLAASWHS NKFLNPARDG AVLPILHLNG YKIANPTILG RANDDDLRRL FEGYGYEPFF
     VDGHEPRDMH QQMAATLDQV FDRIREIQEQ ARSSKAAAGC PRWPMIVLRS LKGWTGPKEV
     DGKKVEGFWR AHQVPVSNCR ENEGHRKILE DWMRSYDPED LFDDEGRLNA DLRALAPVGK
     RRMGASPHAN GGLLRRELDV PDIGDYAVDV GKRGSVVAQS TEILGHYLRD TMKLNAKAAN
     FRIFGPDETE SNRLGSVFDV TNRVWMEDIE PYDVHLSRDG RVMEVLSEHL CQGWLEGYLL
     TGRHGLFSCY EAFIHIIDSM FNQHAKWLKV TRELEWRKPI SSLNYLLTSH VWRQDHNGFS
     HQDPGFVDLV VNKKADIVRI YLPPDANTLL WVGDHCLRTY DRVNVIVAGK QPEPQWLSME
     EAVKHCEAGI GIWRWASNEE DTISPDLVMA CAGDVPTMET LAAVDLLRTA IPELKIRTVN
     VVDLLALQSR DQHPHGLSDE AFDAIFTADK PVIFAYHGYP YLIHRLTYKR TNHENIHVRG
     FIEEGTTTTP FDMTVLNELD RYHLAIEAIE RVPGLKEKAK GAFAAFQGKL AEHHDYVREY
     GEDMPEVRNW TWPAA
//