PTAB_PESFW
ID PTAB_PESFW Reviewed; 313 AA.
AC A0A067XMV3; W3WVS2;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Lactamase-like protein ptaB {ECO:0000303|PubMed:24302702};
DE EC=3.1.2.- {ECO:0000305|PubMed:24302702};
DE AltName: Full=Pestheic acid biosynthesis cluster protein B {ECO:0000303|PubMed:24302702};
GN Name=ptaB {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10825;
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=24302702; DOI=10.1002/cbic.201300626;
RA Xu X., Liu L., Zhang F., Wang W., Li J., Guo L., Che Y., Liu G.;
RT "Identification of the first diphenyl ether gene cluster for pestheic acid
RT biosynthesis in plant endophyte Pestalotiopsis fici.";
RL ChemBioChem 15:284-292(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- FUNCTION: Lactamase-like protein; part of the gene cluster that
CC mediates the biosynthesis of pestheic acid, a diphenyl ether which is a
CC biosynthetic precursor of the unique chloropupukeananes
CC (PubMed:24302702). The biosynthesis initiates from condensation of
CC acetate and malonate units catalyzed by the non-reducing PKS ptaA
CC (PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient,
CC hydrolysis and Claisen cyclization of the polyketide could be catalyzed
CC by ptaB containing a beta-lactamase domain (PubMed:24302702). The ptaB
CC protein might hydrolyze the thioester bond between the ACP of ptaA and
CC the intermediate to release atrochrysone carboxylic acid, which is
CC spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702).
CC Endocrocin anthrone is then converted to endocrocin, catalyzed by the
CC anthrone oxygenase ptaC (PubMed:24302702). Spontaneous decarboxylation
CC of endocrocin occurs to generate emodin (PubMed:24302702). An O-
CC methyltransferase (ptaH or ptaI) could methylate emodin to form
CC physcion (PubMed:24302702). PtaJ could then catalyze the oxidative
CC cleavage of physcion, and rotation of the intermediate could then
CC afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative NADH-
CC dependent oxidoreductase, might also participate in the oxidative
CC cleavage step (PubMed:24302702). Desmethylisosulochrin is then
CC transformed by another O-methyltransferase (ptaH or ptaI) to form
CC isosulochrin (PubMed:24302702). Chlorination of isosulochrin by ptaM in
CC the cyclohexadienone B ring then produces chloroisosulochrin
CC (PubMed:24302702). PtaE is responsible for the oxidative coupling
CC reactions of both benzophenones isosulochrin and chloroisosulochrin to
CC RES-1214-1 and pestheic acid respectively, regardless of chlorination.
CC {ECO:0000269|PubMed:24302702}.
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:24302702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000305|PubMed:24302702};
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:24302702}.
CC -!- INDUCTION: The cluster is expressed in rice fermentation medium
CC (PubMed:25623211). Three regulators are located in the cluster (ptaR1,
CC ptaR2 and ptaR3), suggesting that the production of pestheic acid is
CC controlled by a complex regulatory mechanism (PubMed:24302702).
CC {ECO:0000269|PubMed:25623211, ECO:0000305|PubMed:24302702}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; KC145148; AGO59041.1; -; Genomic_DNA.
DR EMBL; KI912116; ETS76951.1; -; Genomic_DNA.
DR RefSeq; XP_007837597.1; XM_007839406.1.
DR AlphaFoldDB; A0A067XMV3; -.
DR SMR; A0A067XMV3; -.
DR STRING; 1229662.A0A067XMV3; -.
DR EnsemblFungi; ETS76951; ETS76951; PFICI_10825.
DR GeneID; 19275838; -.
DR KEGG; pfy:PFICI_10825; -.
DR eggNOG; KOG0813; Eukaryota.
DR OMA; EGGYRQI; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000030651; 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..313
FT /note="Lactamase-like protein ptaB"
FT /id="PRO_0000443039"
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 313 AA; 34677 MW; B244AC44569B5994 CRC64;
MVGKGGYRQI NKALNICAFE DYLDGQQKSL PPLNDVEQIS PNVLRVLGQN PGKFTLQGTN
TYIIGTGEKR LLIDTGQGIP EWADLISSTL ANSSIRLSAV LLSHWHGDHT GGVPDLLRLY
PHLSDSIYKH SPSKGQQPIE DGQVFEVEGA TVRAVHAPGH SHDHMCFVIE EENAMFTGDN
VLGHGTAAVE LLSTWMATLR LMQSHNCGRG YPAHGEVIPN LNAKISGELA SKERRERQVL
QHLNRIRKEE QGGKGSATVQ RLVVEMYGDT DQQMREQALE PFIDEVLRKL AEDEKVAFQL
RAGEKTWFAI ALE
