ID C1K2N2_METAN Unreviewed; 820 AA.
AC C1K2N2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=Phophoketolase {ECO:0000313|EMBL:ACO24516.1};
GN Name=MPK1 {ECO:0000313|EMBL:ACO24516.1};
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530 {ECO:0000313|EMBL:ACO24516.1};
RN [1] {ECO:0000313|EMBL:ACO24516.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:ACO24516.1};
RX PubMed=19538505; DOI=10.1111/j.1462-2920.2009.01961.x;
RA Duan Z., Shang Y., Gao Q., Zheng P., Wang C.;
RT "A phosphoketolase Mpk1 of bacterial origin is adaptively required for full
RT virulence in the insect-pathogenic fungus Metarhizium anisopliae.";
RL Environ. Microbiol. 11:2351-2360(2009).
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; FJ790496; ACO24516.1; -; mRNA.
DR AlphaFoldDB; C1K2N2; -.
DR VEuPathDB; FungiDB:MAN_08453; -.
DR BRENDA; 4.1.2.9; 3247.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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 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 2: Evidence at transcript level;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 25..383
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 601..802
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 820 AA; 92453 MW; 1FD8FC05D8AB6B93 CRC64;
MADEQSIRAF GPARSTIKGN PLSSSDIALY NDYFKASCYL SLGMIYLRDN PLLREPLNKA
HLKQRLLGHF GSAPGQIFTY MHFNRLIKKY DLNAYFVSGP GHGAPAVLSQ SYLEGVYSEV
YPEKSLDAAG LQKFFKYFSF PGGIGSHATP ETPGSIHEGG ELGYSISHAF GSVFDHPDLI
ALTMVGDGEA ETGPLATSWH STKFLNPITD GAVLPVLHLN GYKINNPTVL ARISHDELKN
LFIGYGWEPF FVEGDELDSM HQAMASTLEH CVRLIKDYQK EARESGKAFR PRWPMIVLRT
PKGWTAPRKV DNNYLGGFWR AHQVPITDVN TNSEHLKVLE NWMRSYEPDR LFDKEGAPVA
ALRALCPEGH RRMSANLVTN GGLIKKPLKM PDFRDYAIKV DQPGATMNGS MTNMAGFLRD
IMALNMHNFR LFGPDETESN KLARVYEAGK KVWMGDYFEE DANGGNLAMA GRVMEMLSEH
TCEGWLEGYI LSGRHGLLNS YEPFIHVIDS MVNQHCKWIE KCLEVEWRAK VASLNILLTA
LVWRQDHNGF THQDPGFLDV VANKSPEVVR IYLPPDGNCL LSVMDHCFRS NNYVNVIVAD
KQDHLQYLDM ESAIQHCTKG IGIWTKFSTD SGCEPDLIMA SCGDISTQES IAAVDLLLNY
FPDLKIRVVN CVDLFKLIHP TDHPHGLTDK EWISIFTENT PIILNFHSYP WMVHRLTYKR
PGSKNLHVRG YREKGNIDTP LELAIRNQTD RFSLAIDAID RMKFLGNRGA SARQALLDQR
IAARNEAFEQ GMDPPALSEW TWQRNGLWQK AAEKLTIHTK
//
