ID E2L521_MONPE Unreviewed; 237 AA.
AC E2L521;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 28-JUN-2023, entry version 32.
DE RecName: Full=Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase N-terminal domain-containing protein {ECO:0000259|Pfam:PF09364};
DE Flags: Fragment;
GN ORFNames=MPER_00836 {ECO:0000313|EMBL:EEB99480.1};
OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS disease fungus) (Marasmius perniciosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB99480.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB99480.1, ECO:0000313|Proteomes:UP000000741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT "A genome survey of Moniliophthora perniciosa gives new insights into
RT Witches' broom disease of cacao.";
RL BMC Genomics 9:548-548(2008).
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:EEB99480.1}.
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DR EMBL; ABRE01002017; EEB99480.1; -; Genomic_DNA.
DR AlphaFoldDB; E2L521; -.
DR STRING; 554373.E2L521; -.
DR KEGG; mpr:MPER_00836; -.
DR HOGENOM; CLU_1197072_0_0_1; -.
DR InParanoid; E2L521; -.
DR OrthoDB; 5485390at2759; -.
DR Proteomes; UP000000741; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
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:SF1; PHOSPHOKETOLASE-RELATED; 1.
DR Pfam; PF09364; XFP_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000741};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 1..193
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT NON_TER 237
FT /evidence="ECO:0000313|EMBL:EEB99480.1"
SQ SEQUENCE 237 AA; 25908 MW; 5DEC7BEE24B255D1 CRC64;
MIFLNNNVLV ERDLTHDDIK PRLLGHWGTC PGLVMIYAHL NRIIRKTGLD ALYVVGPGHG
APGILSCLWL EDSLSNFLPE YSRNLKGLHK LVSGFSVPGG FPSHINAETP GAIHEGGELG
YALSVSFGAV MDKPDLVVTC IVGDGEAETG PTATAWHGFK YIDPAESGAV LPIVHVNGFK
ISERTIYGTM DKYRKLPLYS PDTVIKLDLW RISMISTMTL LRQWSGLGKI KEIQKAA
//