AR282_ARTOA
ID AR282_ARTOA Reviewed; 537 AA.
AC G1XU03;
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_s00215g282 {ECO:0000303|PubMed:28475838};
DE EC=1.-.-.- {ECO:0000305|PubMed:28475838};
DE AltName: Full=Arthrosporol biosynthesis cluster protein AOL_s00215g282 {ECO:0000303|PubMed:28475838};
DE AltName: Full=m-cresol hydroxylase {ECO:0000303|PubMed:27723963};
GN ORFNames=AOL_s00215g282;
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, AND DISRUPTION PHENOTYPE.
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: 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). {ECO:0000269|PubMed:26422178,
CC ECO:0000269|PubMed:27723963, 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:27723963}.
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 m-cresol (PubMed:27723963). Lead to altered growth rates
CC and causes significant decreases in the spore formation and germination
CC (PubMed:27723963). {ECO:0000269|PubMed:27723963}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; ADOT01000316; EGX43546.1; -; Genomic_DNA.
DR RefSeq; XP_011127786.1; XM_011129484.1.
DR AlphaFoldDB; G1XU03; -.
DR SMR; G1XU03; -.
DR STRING; 13349.G1XU03; -.
DR EnsemblFungi; EGX43546; EGX43546; AOL_s00215g282.
DR GeneID; 22898693; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_2_1_1; -.
DR InParanoid; G1XU03; -.
DR OMA; EPCIQQG; -.
DR OrthoDB; 702827at2759; -.
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 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..537
FT /note="Cytochrome P450 monooxygenase AOL_s00215g282"
FT /id="PRO_0000445286"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 451
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 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 537 AA; 61549 MW; 7740992A002A70DF CRC64;
MIPINISPAT VVLCGSIVTV SIAYVIFVVG HRRKGFPPGP PTLPVIGNIH QLPTTGAHFK
FTEWAQKYGG IYSLKLGTGT ALVITDREIV KKLMDKKSSI TSDRPPSYVS YDLITKGDHL
LVMHYNETWR KIRKYMHQFF RESECEKKHI TLQDAEATQM MLEFLETPDN HNLHTKRFSN
SIISTLLFGL RTPTYDSPHA KHLYDIMERW SAVMEPGNTP PVDIYPIFKY IPESLFGNWI
SRASGVGRDM ERLYANMISQ FKIRAEDPKI SRTHESFFDI LLREQEKTRE FTDHEIAFIG
GVQLEGGSDT SASILTAFVQ AMVNWPEVQR VAQEEIDRVI GEDRSPTWND FAALPYINAI
MKETHRWRPV TPLSFPHCLT KDEYLDGFLL PKGATIILNV WGIQNDESVY PRPEEFDPSR
FKDHKLLAPE YAVSDWKLRD HYSFGVGRRI CPGIHLAERN VWLGVAKLLW AFKFEKATGA
DGQPIEMNVD PKTGYTEGFL HCALPFKCKV TVRSEERRKT ILKEFELAKQ VFNEYTG
