ID   PHK_RHOBA               Reviewed;         793 AA.
AC   Q7UH14;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Probable phosphoketolase {ECO:0000255|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_01403};
GN   OrderedLocusNames=RB4903;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294141; CAD78165.1; -; Genomic_DNA.
DR   RefSeq; NP_866384.1; NC_005027.1.
DR   RefSeq; WP_011120163.1; NC_005027.1.
DR   AlphaFoldDB; Q7UH14; -.
DR   SMR; Q7UH14; -.
DR   STRING; 243090.RB4903; -.
DR   EnsemblBacteria; CAD78165; CAD78165; RB4903.
DR   KEGG; rba:RB4903; -.
DR   PATRIC; fig|243090.15.peg.2329; -.
DR   eggNOG; COG3957; Bacteria.
DR   HOGENOM; CLU_013954_2_0_0; -.
DR   InParanoid; Q7UH14; -.
DR   OMA; LSTMDHC; -.
DR   OrthoDB; 45239at2; -.
DR   Proteomes; UP000001025; 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; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..793
FT                   /note="Probable phosphoketolase"
FT                   /id="PRO_0000193888"
SQ   SEQUENCE   793 AA;  89500 MW;  6B85F5EE4D6EC3DC CRC64;
     MIETLESTQV SHETLRTIDA YWRAANYLSV GQIYLSDNPL LKRPLRIEDV KKMLLGHWGT
     TPGQNFIYAH LNRTIKQNDL NMIYVSGPGH GGPAVVANTY LEGSYSEIYP HISQDEAGMR
     KLFVQFSFPG GIPSHASPEC PGSIHEGGEL GYSLSHSFGA VFDNPDLIVA CVVGDGEAET
     GPLATAWHSN KFLNPATDGA VLPILHLNGF KIANPTILAR INHEELEQLM RGYGWTPIFV
     EGKDPMKMHA AMAEALDVAI GQIRSIQQNA RETGDTSRPR WPMIVLRSPK GWTGPKFVDG
     VRNEGTFHSH QVPLSDPAKC PEHLKQIEQW LRSYRPEELL DENGRLRQEI ADLAPTGDRR
     MGANPHANGG RLLRRLKMPD FRDYAVEISQ RGCRGIGDTH VTGKFIRDIV RLNEEHKNFR
     IFGPDETISN GLEAVFDVTQ RQWNAAIVED DESLAPTGRV LEMLSEHQCE GWLEGYLLTG
     RHGLFNCYEA FVHIVDSMFN QHAKWLKVTS ELPWRHKIAS LNYLLASHVW RQDHNGFTHQ
     DPGFLDVVVN KKAEIVRVYL PPDANCLLSV MDHCLRSQHY VNVVVAGKHP SPQWLTMGEA
     AEHCAKGIGI WDWAGNESSS DPDVVMACCG DVPTLETLAA VSILREHLPD LTIRVVNVVD
     LMRLQPKSEH PHGLSDSDFD ALFTKNKHVI FAFHAYPWLV HRLTYRRTNH ANIHVRGYKE
     EGTITTPFDM TVLNDLDRFH LVMDAIDRLP ETGGRGQRLK ALMQEKLVEH RRYINENGQD
     MPEIRDWEWS ARS