ID C1AW20_RHOOB Unreviewed; 800 AA.
AC C1AW20;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase {ECO:0000313|EMBL:BAH49450.1};
DE EC=4.1.2.22 {ECO:0000313|EMBL:BAH49450.1};
DE EC=4.1.2.9 {ECO:0000313|EMBL:BAH49450.1};
GN Name=xfp {ECO:0000313|EMBL:BAH49450.1};
GN OrderedLocusNames=ROP_12030 {ECO:0000313|EMBL:BAH49450.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH49450.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH49450.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH49450.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623}.
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DR EMBL; AP011115; BAH49450.1; -; Genomic_DNA.
DR RefSeq; WP_012688426.1; NC_012522.1.
DR AlphaFoldDB; C1AW20; -.
DR STRING; 632772.ROP_12030; -.
DR KEGG; rop:ROP_12030; -.
DR PATRIC; fig|632772.20.peg.1274; -.
DR HOGENOM; CLU_013954_2_0_11; -.
DR OrthoDB; 9768449at2; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0047905; F:fructose-6-phosphate phosphoketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0050193; F:phosphoketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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:0000313|EMBL:BAH49450.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 17..376
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 596..799
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 800 AA; 87550 MW; E8A39346018ED4C0 CRC64;
MTEVRQPGSQ DSDGHYSDAD LESDLRWWAA ANYLTVAQIY LQDNTLLREP LRPEHIKPRL
LGHWGTSPGL SMIYALLNRL IRRTDTDCLY VTGPGHGGPA LVAATYLEGT YSEVYPGVSR
DAAGIHRLCR QFSTPGGIPS HVSVQTPGSI HEGGELGYAL AHAAGAAFDH PNLLVACVIG
DGEAETGPLS ASWKLPAFLN PERDGAVLPI LHVNGAKIAG PTVHGRSSDA DVEAFLGGQG
WAPVVVSGDD PRQVFPALHR ALTDAHTAIS DLQREARADR RSAAKWPAIV LRTPKGWTGP
RTVDGVLVEG THRAHQVPLS GVRTNEAHLR QLEEWMRSYG PDQLFDSSGA LVPDLVRLAP
QGDKRMGSSP YANGGRLRAD LPVPPLEKYA LPIEKPGTTH HETTRVLGEL LRDLYAATTT
QDGGGYFRLF CPDETSSNRL GAVFEVTDRC WQLPVTDYDD GLAARGRVME VLSEHLCEGW
LEGYLLSGRH GLFASYEAFA MVSVSMLVQH TKWLQHAVDL PWRAPVASLN VLLTSTCWRN
DHNGFSHQGP GMIDAVIPLA PDVVRVWLPP DSNTLLSIAD HCLRSTDHVN LVVVDKQPHL
QYLSLAEAHA HCAAGASVWE WAGTESSAGT EPDVVLAAAG DVPTQEILAA AQLLREHTPE
LVTRVVNVVD LMGLLTPTEH PHGFDARTFL DLFTADTDVV FAFHGYSRAV HELLHGRPAP
DRFHVRGFSE QGTTTTPFDM VVLNRMSRYH LALAALRRTR REPAGATELA DHCLRQLERH
GEYVVAHLED MPEVRDWTWS
//
