AR280_ARTOA
ID AR280_ARTOA Reviewed; 501 AA.
AC G1XU01;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Cytochrome P450 monooxygenase AOL_s00215g280 {ECO:0000303|PubMed:28475838};
DE EC=1.-.-.- {ECO:0000305|PubMed:28475838};
DE AltName: Full=Arthrosporol biosynthesis cluster protein AOL_s00215g280 {ECO:0000303|PubMed:28475838};
GN ORFNames=AOL_s00215g280;
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.
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, DISRUPTION PHENOTYPE, AND PATHWAY.
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of arthrosporols, metabolites that possess a
CC novel hybrid carbon skeleton consisting of a polyketide-derived
CC 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). AOL_s00215g280 is not only involved in the
CC biosynthesis for arthrosporols but also attributed to the regulation in
CC trap formation and fungal predatory ability (PubMed:28475838).
CC {ECO:0000269|PubMed:26422178, ECO:0000269|PubMed:27723963,
CC ECO:0000269|PubMed:28475838}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:28475838}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of arthrosporol A and
CC accumulates three new epoxycyclohexenol/sesquiterpenol hybrids with
CC different oxygenated patterns around the epoxycyclohexone moiety
CC (PubMed:28475838). Leads to a dramatic decrease in the conidial
CC formation but develops numerous traps and kills 85% nematodes
CC (PubMed:28475838). {ECO:0000269|PubMed:28475838}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; ADOT01000316; EGX43544.1; -; Genomic_DNA.
DR RefSeq; XP_011127784.1; XM_011129482.1.
DR AlphaFoldDB; G1XU01; -.
DR SMR; G1XU01; -.
DR STRING; 13349.G1XU01; -.
DR EnsemblFungi; EGX43544; EGX43544; AOL_s00215g280.
DR GeneID; 22898691; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_14_4_1; -.
DR InParanoid; G1XU01; -.
DR OMA; HVIKAFP; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Cytochrome P450 monooxygenase AOL_s00215g280"
FT /id="PRO_0000445285"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 445
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 501 AA; 57127 MW; 2BBD306D3E15A096 CRC64;
MFALSLLLLP LGYIVYLIGL AVYRIWFHPL SKFPGPKAAA VSEYWEAWWN IWPHKGGCLF
EVERLHGVHG AAVRMGPNEI HVNDPRYYHE LYRLGSRYYK DPEMHKVLGA PSSTVAETDP
VLHKIRRGAL EQLFSRQSIL KLEPMIMGKV ERWSSKLEEH FQAGKPVPME FALKSLTMDM
VTTFAFGQEF GAVEDPGFMS IPVRLFRNYL MSLHVIKAFP FVKLLQGLPY FIARHISPTV
EMGRHLEDLS DGHINSFVDK WQNGDKPNFP TVIGRLLTPN EDKGFQVPSK QGIKDEVITL
VSAGNDTTGI TSMVGLFQIL TNPKIYDRLL AELKTILPKV DSVAPYQELE KLPYLTACIK
ESLRYASAAA SRTPRLVPPG GIYLPDGRFV PAGTRIGMAI YLIHFNPDLF PNPRVFDPER
WLRDPAEMTV QNKFLVPFSK GTRACIGINL AHMELYTIMA YLIRRHDLKL YNTTAKDMEW
WDMVIPEFKG TFKAWTGKRT E
