PK81A_PSEFD
ID PK81A_PSEFD Reviewed; 333 AA.
AC M3ANL0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Atrochrysone carboxyl ACP thioesterase MYCFIDRAFT_190111 {ECO:0000303|PubMed:30735556};
DE EC=3.1.2.- {ECO:0000305|PubMed:30735556};
DE AltName: Full=PKS8-1 gene cluster protein MYCFIDRAFT_190111 {ECO:0000303|PubMed:30735556};
GN ORFNames=MYCFIDRAFT_190111;
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: Atrochrysone carboxyl ACP thioesterase; part of the gene
CC cluster that mediates the biosynthesis of an emodin derivative that may
CC be involved in black Sigatoka disease of banana (PubMed:27388157,
CC PubMed:30735556). The pathway begins with the synthesis of atrochrysone
CC thioester by the polyketide synthase PKS8-1 (Probable). The
CC atrochrysone carboxyl ACP thioesterase MYCFIDRAFT_190111 then breaks
CC the thioester bond and releases the atrochrysone carboxylic acid from
CC PKS8-1 (Probable). The decarboxylase MYCFIDRAFT_34057 then catalyzes
CC the concerted decarboxylation-elimination required to convert
CC atochrysone carboxylic acid into emodin anthrone, which is further
CC oxidized to emodin by the anthrone oxygenase MYCFIDRAFT_34418
CC (Probable). The functions of the other tailoring enzymes as well as the
CC final product of the cluster have still to be identified (Probable).
CC {ECO:0000269|PubMed:27388157, ECO:0000269|PubMed:30735556,
CC ECO:0000305|PubMed:30735556}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate +
CC H(+) + holo-[ACP]; Xref=Rhea:RHEA:64236, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:149712, ChEBI:CHEBI:149713;
CC Evidence={ECO:0000305|PubMed:30735556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000305|PubMed:30735556};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q988B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q988B9};
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 metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; KB446562; EME79057.1; -; Genomic_DNA.
DR RefSeq; XP_007929883.1; XM_007931692.1.
DR AlphaFoldDB; M3ANL0; -.
DR SMR; M3ANL0; -.
DR STRING; 83344.XP_007929883.1; -.
DR EnsemblFungi; EME79057; EME79057; MYCFIDRAFT_190111.
DR GeneID; 19335127; -.
DR KEGG; pfj:MYCFIDRAFT_190111; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000016932; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..333
FT /note="Atrochrysone carboxyl ACP thioesterase
FT MYCFIDRAFT_190111"
FT /id="PRO_0000451118"
FT ACT_SITE 112
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ SEQUENCE 333 AA; 37053 MW; 8E02BDCC3A86551B CRC64;
MADQDGDKSG YRQINKALNI CAFDDYLKGQ RAHLPQIPAV EQLTPRVLRV LGQNAGKFTL
QGTNTFIVGK GRDRIIVDTS GGEEEWIELI QETLLDRGIN ITHVLLTHWH GDHTGGVPDL
IRLYPHLKDH IYKNEPERDQ QAIQDGQIFA VQGATIRALH APGHSTDHMC FILEEEHAMF
TGDNILGHGT SAVEDLGTFM ASLQTMADQN CKTGYSAHGV TIDNLPIKIS AELTKLLRRE
KQVLSALAQF RKRGERCAAL RDIVTEIYGQ ALEEDTRRLA LEPFIDEVLR KLAGDGRVAF
QKRGGLKKWY SLEMEMAVDA KAAQVAQARA IAV
