ID   PHK_RHOPS               Reviewed;         784 AA.
AC   Q13B10;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable phosphoketolase {ECO:0000255|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_01403};
GN   OrderedLocusNames=RPD_1492;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01403};
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01403}.
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DR   EMBL; CP000283; ABE38729.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q13B10; -.
DR   SMR; Q13B10; -.
DR   STRING; 316057.RPD_1492; -.
DR   EnsemblBacteria; ABE38729; ABE38729; RPD_1492.
DR   KEGG; rpd:RPD_1492; -.
DR   eggNOG; COG3957; Bacteria.
DR   HOGENOM; CLU_013954_2_0_5; -.
DR   OMA; EHMCQGF; -.
DR   OrthoDB; 45239at2; -.
DR   BioCyc; RPAL316057:RPD_RS07545-MON; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
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; PTHR31273; 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; SSF52518; 2.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase; Thiamine pyrophosphate.
FT   CHAIN           1..784
FT                   /note="Probable phosphoketolase"
FT                   /id="PRO_1000145458"
SQ   SEQUENCE   784 AA;  88185 MW;  A605C8DBA9FE2457 CRC64;
     MFDVLSDDLM QKMDAYWRAA NYLSVGQIYL QDNPLLEQPL RIEHIKPRLL GHWGTTPGLN
     LLYVHLNRLI SAHDLDMIYI IGPGHGGPGL VANSYLEGSY TERYPAIERN RNGLQRLFRQ
     FSWPNGVPSH VSPETPGSIH EGGELGYSLA HAYGAAFDNP DLIVACIVGD GEAETGALAT
     SWHSNKFLNP ARDGAVLPIL HLNGFKIANP TILARIGRQE LTDLMRGYGY EPIVVEGDDP
     KLVHHTLAAA LERALADIRA IQAAARHQGV TVRPRWPMII LRTPKGWTGP KQVDGKQIEG
     TWRAHQVPIA SFKDPTHVQL LETWLRSYRP EELFDASGKF RDDLAALAPT GHRRMSANPH
     ANGGELLQPL SLPDFHDYAV TQSGPGTVKA EATRVLGAFL RDVMKSNLDA KNFRLFGPDE
     TASNRLDAVL EVTDKEWMAE IEDVDVALGP DGRVMEVLSE HLCQGWLEGY LLTGRHGFFS
     CYEAFIHIVG SMFNQHAKWL KTCDAIPWRR PIASLNYLLT SHVWRQDHNG LSHQDPGFID
     HVVNKKASVV RVYLPPDANC LLSVADHCLR SRNYVNLIVA GKQPEWQWLD IDSAVRHCSA
     GAGIWHWASN GEDDPDVVMA CAGDVPTLET LAAVMLLREY VPDIRVRVVN VVDLMVLQPS
     SEHPHGLDDK RFDEIFTVDK PVVFAFHGYP WLIHRLTYRR RNHFNIHVRG YKEEGSTTTP
     FDMVVLNDLD RYRLALDAIR RIPRLAGEVE AATARYWATM QRHKLYIGEH GDDMPEVRDW
     SWQG