ID   K5DZL2_RHOBT            Unreviewed;       793 AA.
AC   K5DZL2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   ORFNames=RBSH_05806 {ECO:0000313|EMBL:EKJ98910.1};
OS   Rhodopirellula baltica SH28.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=993517 {ECO:0000313|EMBL:EKJ98910.1, ECO:0000313|Proteomes:UP000007993};
RN   [1] {ECO:0000313|EMBL:EKJ98910.1, ECO:0000313|Proteomes:UP000007993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH28 {ECO:0000313|EMBL:EKJ98910.1,
RC   ECO:0000313|Proteomes:UP000007993};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA   Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT   sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKJ98910.1}.
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DR   EMBL; AMCW01000167; EKJ98910.1; -; Genomic_DNA.
DR   RefSeq; WP_007335141.1; NZ_AMCW01000167.1.
DR   AlphaFoldDB; K5DZL2; -.
DR   PATRIC; fig|993517.3.peg.6289; -.
DR   Proteomes; UP000007993; Unassembled WGS sequence.
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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
FT   DOMAIN          10..371
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          588..789
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   793 AA;  89694 MW;  86FA4914D6902DF2 CRC64;
     MIETLESTQV SPETLQTIDA YWRAANYLSV GQIYLSDNPL LKRPLRIEDV KKMLLGHWGT
     TPGQNFIYAH LNRTIKQNDL NMIYVSGPGH GGPAVVANTY SEGSYSEIYP HISQDEAGMR
     KLFVQFSFPG GIPSHASPEC PGSIHEGGEL GYSLSHSFGA VFDNPDLIVA CVVGDGEAET
     GPLATAWHSN KFLNPATDGA VLPILHLNGF KIANPTILAR INHEELEQLM RGYGWTPIFV
     EGEDPMKMHA AMAEALDVAI EQIRSIQQNA RETGDTSRPR WPMIVLRSPK GWTGPKFVDG
     VRNEGTFHSH QVPLSDPAKC PEHLKQIERW LRGYRPEELF DENGRLRQEI ADLAPTGDRR
     MGANPHANGG RLLRRLKMPD FRDYAVEITQ RGCRGIGDTH VTGKFIRDIV QLNEEHKNFR
     IFGPDETISN GLEAVFDVTQ RQWNAAIVED DESLAPTGRV LEMLSEHQCE GWLEGYLLTG
     RHGLFNCYEA FVHIVDSMFN QHAKWLKVTS ELPWRHKIAS LNYLLASHVW RQDHNGFTHQ
     DPGFLDVVVN KKAEIVRVYL PPDANCLLSV MDHCLRSQHY VNVVVAGKHP SPQWLTMDEA
     AEHCAKGIGI WDWAGNESSS DPDVVMACCG DVPTLETLAA VSILREHLPD LTIRVVNVVD
     LMRLQPKSEH PHGLSDPNFD DLFTKNKHVI FAFHAYPWLV HRLTYRRTNH ANIHVRGYKE
     EGTITTPFDM TVLNDLDRFH LVMDVIDRLP ETGERGQRLK ALMQEKLVEH RRYINQNGQD
     MPEVRDWEWS ARS
//