PK81G_PSEFD
ID PK81G_PSEFD Reviewed; 296 AA.
AC M3APK9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Aldo-keto reductase MYCFIDRAFT_156381 {ECO:0000303|PubMed:30735556};
DE EC=1.-.-.- {ECO:0000305|PubMed:30735556};
DE AltName: Full=PKS8-1 gene cluster protein MYCFIDRAFT_156381 {ECO:0000303|PubMed:30735556};
GN ORFNames=MYCFIDRAFT_156381;
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=27388157; DOI=10.1371/journal.pone.0158471;
RA Noar R.D., Daub M.E.;
RT "Bioinformatics prediction of polyketide synthase gene clusters from
RT Mycosphaerella fijiensis.";
RL PLoS ONE 11:e0158471-e0158471(2016).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30735556; DOI=10.1371/journal.pone.0212229;
RA Noar R.D., Thomas E., Daub M.E.;
RT "A novel polyketide synthase gene cluster in the plant pathogenic fungus
RT Pseudocercospora fijiensis.";
RL PLoS ONE 14:e0212229-e0212229(2019).
CC -!- FUNCTION: Aldo-keto reductase; part of the gene cluster that mediates
CC the biosynthesis of an emodin derivative that may be involved in black
CC Sigatoka disease of banana (PubMed:27388157, PubMed:30735556). The
CC pathway begins with the synthesis of atrochrysone thioester by the
CC polyketide synthase PKS8-1 (Probable). The atrochrysone carboxyl ACP
CC thioesterase MYCFIDRAFT_190111 then breaks the thioester bond and
CC releases the atrochrysone carboxylic acid from PKS8-1 (Probable). The
CC decarboxylase MYCFIDRAFT_34057 then catalyzes the concerted
CC decarboxylation-elimination required to convert atochrysone carboxylic
CC acid into emodin anthrone, which is further oxidized to emodin by the
CC anthrone oxygenase MYCFIDRAFT_34418 (Probable). The functions of the
CC other tailoring enzymes as well as the final product of the cluster
CC have still to be identified (Probable). {ECO:0000269|PubMed:27388157,
CC ECO:0000269|PubMed:30735556, ECO:0000305|PubMed:30735556}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30735556}.
CC -!- INDUCTION: Does not seem to be up-regulated during banana leaves
CC infection. {ECO:0000269|PubMed:30735556}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; KB446562; EME79063.1; -; Genomic_DNA.
DR RefSeq; XP_007929887.1; XM_007931696.1.
DR AlphaFoldDB; M3APK9; -.
DR SMR; M3APK9; -.
DR STRING; 83344.XP_007929887.1; -.
DR EnsemblFungi; EME79063; EME79063; MYCFIDRAFT_156381.
DR GeneID; 19331854; -.
DR KEGG; pfj:MYCFIDRAFT_156381; -.
DR eggNOG; ENOG502QU2T; Eukaryota.
DR HOGENOM; CLU_023205_1_1_1; -.
DR OrthoDB; 1226539at2759; -.
DR Proteomes; UP000016932; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 2: Evidence at transcript level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..296
FT /note="Aldo-keto reductase MYCFIDRAFT_156381"
FT /id="PRO_0000451124"
FT ACT_SITE 19
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 113..114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 139
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 168..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 255..263
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT SITE 47
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O43488"
SQ SEQUENCE 296 AA; 33274 MW; 013E468BC352D4FB CRC64;
MLDTLQKHGH CEVDTARIYG FGSTEEHLAQ LKWQERGIAV GTKLTAKKIG PKEYSHKKES
LKPGLSESLK ALGSERVDTF YLHTPDHNTP YAETLEAVNE LYKAGYFKKF GICNYAAWEV
AQICELCNAN GWKKPDIYQG AYSALQRNIE TELFPCLRYY GISFYSFSPL AGGMLTDRYG
RETSEYEGGN RFDPNNARGF YRKLYWNEPT FAALDIIRPL AQKHGMTTTK AALRWISHHS
AMKGDKGDAV VIGSSSAEQL ESNLSNLEKG PLPEDLVQAF EEAWSVVKVN TAPYFA
