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Database: UniProt
Entry: I4VWI1_9GAMM
LinkDB: I4VWI1_9GAMM
Original site: I4VWI1_9GAMM 
ID   I4VWI1_9GAMM            Unreviewed;       799 AA.
AC   I4VWI1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   ORFNames=UU9_03902 {ECO:0000313|EMBL:EIL91572.1};
OS   Rhodanobacter fulvus Jip2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL91572.1, ECO:0000313|Proteomes:UP000004210};
RN   [1] {ECO:0000313|EMBL:EIL91572.1, ECO:0000313|Proteomes:UP000004210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(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:EIL91572.1}.
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DR   EMBL; AJXU01000018; EIL91572.1; -; Genomic_DNA.
DR   RefSeq; WP_007080421.1; NZ_AJXU01000018.1.
DR   AlphaFoldDB; I4VWI1; -.
DR   STRING; 1163408.UU9_03902; -.
DR   PATRIC; fig|1163408.3.peg.800; -.
DR   eggNOG; COG3957; Bacteria.
DR   OrthoDB; 9768449at2; -.
DR   Proteomes; UP000004210; 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   Reference proteome {ECO:0000313|Proteomes:UP000004210};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
FT   DOMAIN          11..372
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          589..790
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   799 AA;  89039 MW;  A2170F32915D395F CRC64;
     MIDLPDQQPV DASQLRAIDA WWRAANYLSV GQIYLRANPL LRQPLAPAHI KRMLLGHWGT
     TPGQNFIYAH LNRAIRQYDL DMVYLSGPGH GGPAVVANAW LEGTYSEVYP QVSQDEAGLQ
     RLFKQFSFPG GIPSHASPEC PGSMHEGGEL GYSLSHAFGA VFDNPGLIAA CVIGDGEAET
     GPLATAWHSN KFLDPVGDGA VLPILHLNGY KIANPAVLAR IGREELEQLL RGYGWMPYFV
     VGSDPVAMHQ AMAAALDAAV VQISQIQRDA REGGACTRPR WPMIVLESPK GWTGPAMVDG
     RPNEGTFRAH QVPLSISPTS PPEHLPQLEA WLRSYRPEQL FDERGRLRPE WAALAPSGAR
     RMSANPHSNG GLLLRDLLLP DFRDYAVAAP QPGARGNGDT RALGPFLRDV IRLNEPSRNF
     RVFGPDETIS NGLAAVFEAT NRQWQAALKP DDEFLAPQGR VVEMLSEHQC EGWLEGYLLT
     GRHGLFNCYE AFIHIVDSMF NQHAKWLKMT AAIPWRRPLA SLNYLLASHV WRQDHNGFTH
     QDPGFIDHVV NKKASIVRVY LPPDANCLLS VMDHCLRSRH YVNVVVAGKH PAPQWLPMDA
     AASHCAQGIG LWPWASSDAH GEPDVVMACA GDVPTLETLA AVSILRRYLP DLKLRVVNVV
     DLMKLQAPSE HPHGLDDDDF DQLFTRDKPV IFAYHGYPSL IHRLTYRRAN HDNLHVHGYR
     EEGTITTAFD MTVLNELDRF HLVIDVINRV PQAGERGVYL KQKLLDKLIE HKHYIDEHGE
     DLPEIRHWMW DAPEAGTLD
//
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