ID   V8RDD2_9PSED            Unreviewed;       789 AA.
AC   V8RDD2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, 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=PMO01_12105 {ECO:0000313|EMBL:ETF09673.1};
OS   Pseudomonas moraviensis R28-S.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395516 {ECO:0000313|EMBL:ETF09673.1};
RN   [1] {ECO:0000313|EMBL:ETF09673.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R28-S {ECO:0000313|EMBL:ETF09673.1};
RX   PubMed=24558233;
RA   Hunter S.S., Yano H., Loftie-Eaton W., Hughes J., De Gelder L.,
RA   Stragier P., De Vos P., Settles M.L., Top E.M.;
RT   "Draft Genome Sequence of Pseudomonas moraviensis R28-S.";
RL   Genome Announc. 2:e00035-14(2014).
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:ETF09673.1}.
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DR   EMBL; AYMZ01000003; ETF09673.1; -; Genomic_DNA.
DR   RefSeq; WP_024012778.1; NZ_CM002330.1.
DR   AlphaFoldDB; V8RDD2; -.
DR   PATRIC; fig|1395516.4.peg.2462; -.
DR   eggNOG; COG3957; Bacteria.
DR   HOGENOM; CLU_013954_2_0_6; -.
DR   Proteomes; UP000024771; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
FT   DOMAIN          6..366
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          583..783
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   789 AA;  88666 MW;  4CD2C0A3E208AEBA CRC64;
     MGDFLDTEQL QGLDAYWRAS NYLAVGQIYL KDNPLLREPL TLAHIKPRLL GHWGTTPGLN
     LIYTHLNRVI KHYDLNMLFV AGPGHGGPAV VAQTWLEGTY TECYPAVERN INGLQRLFRQ
     FSWPYGISSH VSAQVPGSIH EGGELGYSLA HAYGAAFDNP DLIVACVIGD GEAETGTLAA
     SWHSNKFLDP ARDGAVLPIL HLNGYKIANP TILSCISEDE LSALMYGYGY DPYFVEGDDP
     QRVHQDLART LDTIIGKIRD IQYQARQASA SVERPLWPML ILRTPKGWTG PKFVDGHRVE
     GTWRAHQVPL ADFRNALHVR QLEDWMNSYR PDELFDDSGA LLPELAALAP TGRRRMSANP
     HGNGGLLLQP LDLPRFTGHG VNLPAPGALR AEATRVLGTY LRDVMKGNLQ SGNFRLFGPD
     ETASNRLDAV YEVTAKAWME PLQEEDINLA PDGRVMEILS EQVCEGWLEG YLLTGRHGLL
     SCYEAFIHIV DSMVSQHAKW LKTAAEVPWR EPIASLNFLL TSHVWRQDHN GFSHQDPGFI
     DLLANKKSAI VRIYLPPDAN CLLSVVDHCL NSRNYINVVV AGKQPEWQWL DIDAAVRHCH
     AGVGRWEWAS HDDEQPDVVM ACAGDVPTLE TLAAVTLLRS HVPDLRVRVV NVVDLMVLQP
     GSQHPHGLSD SAFDELFTID RPVIFAFHGY PALIHRLLYK RTNHDNFHVR GFKEEGATTT
     PFDMAVINNL DRYQLALDVI ERVPRFHELV ETARARYWSM MEKHKLYLIE HGEDLPEVRN
     WQWTPAVVH
//