CLAF_PASFU
ID CLAF_PASFU Reviewed; 333 AA.
AC P0CU68;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000303|PubMed:27274078};
DE Short=ACTE {ECO:0000250|UniProtKB:Q5BH31};
DE EC=3.1.2.- {ECO:0000269|PubMed:27274078};
DE AltName: Full=Cladofulvin biosynthesis cluster protein F {ECO:0000303|PubMed:27274078};
GN Name=claF {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184396;
OS Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX NCBI_TaxID=5499;
RN [1]
RP IDENTIFICATION, FUNCTION, AND INDUCTION.
RX PubMed=24465762; DOI=10.1371/journal.pone.0085877;
RA Collemare J., Griffiths S., Iida Y., Karimi Jashni M., Battaglia E.,
RA Cox R.J., de Wit P.J.;
RT "Secondary metabolism and biotrophic lifestyle in the tomato pathogen
RT Cladosporium fulvum.";
RL PLoS ONE 9:E85877-E85877(2014).
RN [2]
RP INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27274078; DOI=10.1073/pnas.1603528113;
RA Griffiths S., Mesarich C.H., Saccomanno B., Vaisberg A., De Wit P.J.,
RA Cox R., Collemare J.;
RT "Elucidation of cladofulvin biosynthesis reveals a cytochrome P450
RT monooxygenase required for anthraquinone dimerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:6851-6856(2016).
RN [3]
RP INDUCTION.
RX PubMed=27997759; DOI=10.1111/mpp.12527;
RA Griffiths S., Mesarich C.H., Overdijk E.J.R., Saccomanno B.,
RA de Wit P.J.G.M., Collemare J.;
RT "Down-regulation of cladofulvin biosynthesis is required for biotrophic
RT growth of Cladosporium fulvum on tomato.";
RL Mol. Plant Pathol. 19:369-380(2018).
CC -!- FUNCTION: Atrochrysone carboxyl ACP thioesterase; part of the gene
CC cluster that mediates the biosynthesis of the bianthraquinone
CC cladofulvin, a conidial pigment not required for virulence but that
CC plays a role in fitness and resistance to environmental stresses
CC including UV light and low-temperature stress (PubMed:24465762,
CC PubMed:27274078). The pathway begins with the synthesis of atrochrysone
CC thioester by the polyketide synthase (PKS) claG. The atrochrysone
CC carboxyl ACP thioesterase claF then breaks the thioester bond and
CC releases the atrochrysone carboxylic acid from claG (PubMed:27274078).
CC This compound is decarboxylated by claH to yield emodin, which is
CC further converted to chrysophanol hydroquinone by the reductase claC
CC and the dehydratase claB (PubMed:27274078). The cytochrome P450
CC monooxygenase claM then catalyzes the dimerization of nataloe-emodin to
CC cladofulvin (PubMed:27274078). {ECO:0000269|PubMed:24465762,
CC ECO:0000269|PubMed:27274078}.
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:0000269|PubMed:27274078};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000269|PubMed:27274078};
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: Pigment biosynthesis. {ECO:0000269|PubMed:27274078}.
CC -!- INDUCTION: Expression is down-regulated during biotrophic growth within
CC tomato leaves (PubMed:27997759). The expression is induced at later
CC stages of infection when conidiophores emerge from the plant and
CC produce conidia (PubMed:24465762). {ECO:0000269|PubMed:24465762,
CC ECO:0000269|PubMed:27997759}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0CU68; -.
DR SMR; P0CU68; -.
DR OMA; EENSMFT; -.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..333
FT /note="Atrochrysone carboxyl ACP thioesterase"
FT /id="PRO_0000445888"
FT ACT_SITE 108
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 104
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 106
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 108
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 109
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; 36853 MW; B12D515C2B2CA38B CRC64;
MDDKGGYRQI NSAFNACAFD DILGSQMAQL PELPDVEQLT PRVLRILGQN PGKFTFQGTN
TYVIGTGRQR LIIDTGGGEA DWASLINDTL KARGITIARV LLTHWHGDHT GGVADLIRLY
PDLEHHIYKN QPDRGQQNIY HAQTFDVEGA TVRALHTPGH SEDHMCFILE EEGEPRAMFT
GDTILGHGTS TMEDLSSFMD SLQNITDQQC EVGYSAHGAV IENLPLKMVQ ELRHKTRREA
QVLTALASYA SRGQRSLTTS ELVAEIYGQS LNAETRAFAL EPFIDQVLRK LAGDGKVGFE
VRAGQRKWFI MDMMQGSIRP ARSGSAREIL VAA
