AR281_ARTOA
ID AR281_ARTOA Reviewed; 325 AA.
AC G1XU02;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=6-methylsalicylic acid decarboxylase {ECO:0000303|PubMed:27723963};
DE EC=4.1.1.52 {ECO:0000269|PubMed:27723963};
DE AltName: Full=Arthrosporol biosynthesis cluster protein AOL_s00215g281 {ECO:0000303|PubMed:27723963};
GN ORFNames=AOL_s00215g281;
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491;
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
RN [2]
RP FUNCTION.
RX PubMed=26422178; DOI=10.1021/acs.jafc.5b04244;
RA Xu Z.F., Wang B.L., Sun H.K., Yan N., Zeng Z.J., Zhang K.Q., Niu X.M.;
RT "High trap formation and low metabolite production by disruption of the
RT polyketide synthase gene involved in the biosynthesis of arthrosporols from
RT nematode-trapping fungus Arthrobotrys oligospora.";
RL J. Agric. Food Chem. 63:9076-9082(2015).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27723963; DOI=10.1021/acs.jafc.6b03241;
RA Xu Z., Chen Y., Song T., Zeng Z., Yan N., Zhang K., Niu X.;
RT "Nematicidal key precursors for the biosynthesis of morphological
RT regulatory arthrosporols in nematode-trapping fungus Arthrobotrys
RT oligospora.";
RL J. Agric. Food Chem. 64:7949-7956(2016).
RN [4]
RP FUNCTION.
RX PubMed=28475838; DOI=10.1021/acs.jafc.7b01290;
RA Song T.Y., Xu Z.F., Chen Y.H., Ding Q.Y., Sun Y.R., Miao Y., Zhang K.Q.,
RA Niu X.M.;
RT "Potent nematicidal activity and new hybrid metabolite production by
RT disruption of a cytochrome P450 gene involved in the biosynthesis of
RT morphological regulatory arthrosporols in nematode-trapping fungus
RT Arthrobotrys oligospora.";
RL J. Agric. Food Chem. 65:4111-4120(2017).
CC -!- FUNCTION: 6-methylsalicylic acid decarboxylase; part of the gene
CC cluster that mediates the biosynthesis of arthrosporols, metabolites
CC that possess a novel hybrid carbon skeleton consisting of a polyketide-
CC derived epoxycyclohexenol combined with a terpenoid-derived monocyclic
CC sesquiterpenol substructure. Arthrosporols B and C are two dehydration
CC derivatives of arthrosporol A. All of the arthrosporols shared the same
CC epoxycyclohexenol moiety, and the difference among them only occurred
CC in the monocyclic sesquiterpenol substructure (PubMed:26422178,
CC PubMed:27723963). The pathway begins with the biosynthesis of 6-
CC methylsalicylic acid (6-MSA), the first precursor of the polyketide-
CC derived epoxycyclohexenol in arthrosporols, by the polyketide synthase
CC (PKS) AOL_s00215g283 via condensation of 1 acetate and 3 malonate
CC units. AOL_s00215g283 performs a series of programmed reactions
CC including Claisen condensation, dehydration, reduction, and cyclization
CC to yield 6-MSA (PubMed:26422178). The 6-methylsalicylic acid
CC decarboxylase AOL_s00215g281 then catalyzes the decarboxylation of 6-
CC methylsalicylic acid to yield m-cresol (PubMed:27723963). The
CC arthrosporols precursor m-cresol might be a versatile precursor for
CC other pathways (PubMed:27723963). The cytochrome P450 monooxygenase
CC AOL_s00215g282 then acts as a m-cresol hydrolase that converts m-cresol
CC to arthrosporols, in combination with other arthrosporols cluster's
CC enzymes such as the cytochrome P450 AOL_s00215g280 (PubMed:27723963,
CC PubMed:28475838). {ECO:0000269|PubMed:26422178,
CC ECO:0000269|PubMed:27723963, ECO:0000269|PubMed:28475838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2;
CC Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52;
CC Evidence={ECO:0000269|PubMed:27723963};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113;
CC Evidence={ECO:0000269|PubMed:27723963};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27723963}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8TDX5}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of arthrosporol A and
CC accumulates 6-methylsalicylic acid (PubMed:27723963). Leads to altered
CC growth rates and the development of much more fluffy aerial hypha
CC (PubMed:27723963). {ECO:0000269|PubMed:27723963}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; ADOT01000316; EGX43545.1; -; Genomic_DNA.
DR RefSeq; XP_011127785.1; XM_011129483.1.
DR AlphaFoldDB; G1XU02; -.
DR SMR; G1XU02; -.
DR STRING; 13349.G1XU02; -.
DR EnsemblFungi; EGX43545; EGX43545; AOL_s00215g281.
DR GeneID; 22898692; -.
DR eggNOG; KOG4245; Eukaryota.
DR HOGENOM; CLU_039329_2_1_1; -.
DR InParanoid; G1XU02; -.
DR OMA; PMIDYPH; -.
DR OrthoDB; 1119055at2759; -.
DR BRENDA; 4.1.1.52; 15923.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0047596; F:6-methylsalicylate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..325
FT /note="6-methylsalicylic acid decarboxylase"
FT /id="PRO_0000445287"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
SQ SEQUENCE 325 AA; 36066 MW; F8A893D22D0C6AFF CRC64;
MSQHPTKFDV HHHFVPDFYV EALEANGGDP SGWTIPKWTL ESSETLMENI GIGTTIFSMT
APGPSIHKDP SEAASLARKT NTFAAAVRDS NPQKFGFFAA LPSLLNKESA ISEIRYAIDE
LKADGVTLFT RYGPDNHYLG HPDFQEIWQE LNDRSAVVFV HPTHGVDTNL VAPSLPQPMI
DYPHETTRTA MDIILSGTVR KYKNCKIILS HAGGTLPYLA LRVAAMMPHT PFGKSNGLST
DEIIEDAKSF YFDLALSGNE FTLGLLLKFA KPGHILFGSD FPYAPTKGIE YFTESFDKYE
FSEEERAAIN RGNAEALFPR FQVAQ
