PK81H_PSEFD
ID PK81H_PSEFD Reviewed; 362 AA.
AC M2YMU7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Aldo-keto reductase MYCFIDRAFT_87468 {ECO:0000303|PubMed:30735556};
DE EC=1.1.1.- {ECO:0000305|PubMed:30735556};
DE AltName: Full=PKS8-1 gene cluster protein MYCFIDRAFT_87468 {ECO:0000303|PubMed:30735556};
GN ORFNames=MYCFIDRAFT_87468;
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: Expression is positively regulated by the cluster-specific
CC transcription factor MYCFIDRAFT_198930 and is up-regulated during
CC banana leaves infection. {ECO:0000269|PubMed:30735556}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; KB446562; EME79065.1; -; Genomic_DNA.
DR RefSeq; XP_007929888.1; XM_007931697.1.
DR AlphaFoldDB; M2YMU7; -.
DR SMR; M2YMU7; -.
DR STRING; 383855.M2YMU7; -.
DR EnsemblFungi; EME79065; EME79065; MYCFIDRAFT_87468.
DR GeneID; 19342584; -.
DR KEGG; pfj:MYCFIDRAFT_87468; -.
DR eggNOG; KOG1575; Eukaryota.
DR HOGENOM; CLU_023205_2_0_1; -.
DR OrthoDB; 1383971at2759; -.
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..362
FT /note="Aldo-keto reductase MYCFIDRAFT_87468"
FT /id="PRO_0000451125"
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT BINDING 210..211
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 236
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 265..275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT BINDING 322..330
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O43488"
SQ SEQUENCE 362 AA; 40954 MW; FB8457A04432D978 CRC64;
MSPMAIEPAG DPEHGAFDRN DNADAVVRSI NETHVTYKRL GKTGLRVSVP ILGCMSLGDK
HWVPWALEED KALPLLKGAF DLGLNCWDTA NVYSNGKSEE IIGKAIKTYQ LPRHKLVLLS
KCGGYVGEAP NVKGDRYENA ISRSKDYVNQ GGLSRSAIFE QVEASLRRLD TTYLDVLQIH
RFDPNTPIEE TMKALHDLVS IGKVRYLGAC SMYTYQFAQM QFVAEKNGWT KFVSMQNHYS
LLYREEERDM IRFCNETGVG LIPWAPLASG MLTRPATQKV PEGDRAIINR VQEVAEKRGW
RMSYVALSWI NKRVSAPVID FDRIDRIEEA LATKDKELTA EEEKYVEELY KAKDVEGIPS
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