CLAM_PASFU
ID CLAM_PASFU Reviewed; 538 AA.
AC P0CU70;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Cytochrome P450 monooxygenase claM {ECO:0000303|PubMed:27274078};
DE EC=1.14.13.- {ECO:0000269|PubMed:27274078};
DE AltName: Full=Cladofulvin biosynthesis cluster protein M {ECO:0000303|PubMed:27274078};
GN Name=claM {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184398;
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 INDUCTION.
RX PubMed=24521437; DOI=10.1111/mmi.12535;
RA Okmen B., Collemare J., Griffiths S., van der Burgt A., Cox R.,
RA de Wit P.J.;
RT "Functional analysis of the conserved transcriptional regulator CfWor1 in
RT Cladosporium fulvum reveals diverse roles in the virulence of plant
RT pathogenic fungi.";
RL Mol. Microbiol. 92:10-27(2014).
RN [2]
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 [3]
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 [4]
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the bianthraquinone cladofulvin, a
CC conidial pigment not required for virulence but that plays a role in
CC fitness and resistance to environmental stresses including UV light and
CC low-temperature stress (PubMed:24465762, PubMed:27274078). The pathway
CC begins with the synthesis of atrochrysone thioester by the polyketide
CC synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF
CC then breaks the thioester bond and releases the atrochrysone carboxylic
CC acid from claG (PubMed:27274078). This compound is decarboxylated by
CC claH to yield emodin, which is further converted to chrysophanol
CC hydroquinone by the reductase claC and the dehydratase claB
CC (PubMed:27274078). The cytochrome monooxygenase P450 claM then
CC catalyzes the dimerization of nataloe-emodin to cladofulvin
CC (PubMed:27274078). {ECO:0000269|PubMed:24465762,
CC ECO:0000269|PubMed:27274078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 nataloe emodin + O2 + reduced [NADPH--hemoprotein reductase]
CC = cladofulvin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:64288, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:152055,
CC ChEBI:CHEBI:152057; Evidence={ECO:0000269|PubMed:27274078};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64289;
CC Evidence={ECO:0000269|PubMed:27274078};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:27274078}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the transcriptional
CC regulator wor1 (PubMed:24521437, PubMed:27274078). Expression is down-
CC regulated during biotrophic growth within tomato leaves
CC (PubMed:27997759). The expression is induced at later stages of
CC infection when conidiophores emerge from the plant and produce conidia
CC (PubMed:24465762). {ECO:0000269|PubMed:24465762,
CC ECO:0000269|PubMed:24521437, ECO:0000269|PubMed:27274078,
CC ECO:0000269|PubMed:27997759}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR AlphaFoldDB; P0CU70; -.
DR SMR; P0CU70; -.
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; 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 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Cytochrome P450 monooxygenase claM"
FT /id="PRO_0000445890"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 472
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 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 538 AA; 60609 MW; 918D726A53FE3860 CRC64;
MNSTAANVKP EPGLYGPDAA ASPAIARYLI QGPSPLSIGL VVLIGAISSF LLQQFLKPAV
NPLSPKFTSN TWPWLGSLGM MIGHWTFWKS CIKESKTGQF SFWLGRTHVV GLSGPDARKM
FFEHPALDLH KATDLTPLGV NFWPIHAIFT PRDEKFQKST YWLRTLTHLM KTPNMERCLP
GVIQDARTGL EALKRDTPSG IINTPKVWPV VFKQTARVFM ADDVTDDPKL WATTLGAIDT
ILHTFSPFNT LLPWIPEPSM IRRRMARRAL LRVSRGIVRD RHASPKSASK NDAVQSLINL
GDPDDNISEF MINAAFVGVV NAHVIFPQLL NALAVHLDWQ DKVYKEVTEV ADQHCKEQCL
PLVDKLFHIP LSAWENSFPN AALMMEEISR IWTCFPTARF NTLYESIPIP GTSEVIPART
HAIYNSTEIH FNPKLYDRPA SFRPDRFAPE SQKTWDKEPH GLNTWGTGQR LCSGMRWAKL
QQNILMAVAL SLYRLEKCDK DGKPDPSAYE KQQAMDGDLD EEVAFVLPEC FVKLIPRE
