PIG18_CLAP2
ID PIG18_CLAP2 Reviewed; 534 AA.
AC M1W266;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Cytochrome P450 monooxygenase CPUR_05419 {ECO:0000303|PubMed:30394754};
DE EC=1.14.13.- {ECO:0000250|UniProtKB:A0A2I1C3T4};
DE AltName: Full=Ergochrome gene cluster protein CPUR_05419 {ECO:0000303|PubMed:30394754};
GN ORFNames=CPUR_05419;
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1;
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
RN [2]
RP FUNCTION.
RX PubMed=28955461; DOI=10.1186/s40694-016-0020-z;
RA Neubauer L., Dopstadt J., Humpf H.U., Tudzynski P.;
RT "Identification and characterization of the ergochrome gene cluster in the
RT plant pathogenic fungus Claviceps purpurea.";
RL Fungal Biol. Biotechnol. 3:2-2(2016).
RN [3]
RP IDENTIFICATION.
RX PubMed=30394754; DOI=10.1021/acs.orglett.8b03123;
RA Matsuda Y., Gotfredsen C.H., Larsen T.O.;
RT "Genetic characterization of neosartorin biosynthesis provides insight into
RT heterodimeric natural product generation.";
RL Org. Lett. 20:7197-7200(2018).
RN [4]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=30996871; DOI=10.1039/c8sc05126g;
RA Greco C., de Mattos-Shipley K., Bailey A.M., Mulholland N.P., Vincent J.L.,
RA Willis C.L., Cox R.J., Simpson T.J.;
RT "Structure revision of cryptosporioptides and determination of the genetic
RT basis for dimeric xanthone biosynthesis in fungi.";
RL Chem. Sci. 10:2930-2939(2019).
RN [5]
RP FUNCTION.
RX PubMed=32105084; DOI=10.1021/acs.orglett.0c00285;
RA Wei X., Matsuda Y.;
RT "Unraveling the fungal strategy for tetrahydroxanthone biosynthesis and
RT diversification.";
RL Org. Lett. 22:1919-1923(2020).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the ergochrome gene
CC cluster responsible for the typical purple-black color of the ergot
CC sclerotia (PubMed:30996871, PubMed:32105084). The ergochrome gene
CC cluster produces several ergot pigments including the yellow ergochrome
CC secalonic acid and its derivatives, as well as the red anthraquinones
CC endocrocin and clavorubin (PubMed:28955461). The pathway begins with
CC the synthesis of atrochrysone thioester by the polyketide synthase
CC (PKS) CPUR_05437 (By similarity). The atrochrysone carboxyl ACP
CC thioesterase CPUR_05436 then breaks the thioester bond and releases the
CC atrochrysone carboxylic acid from CPUR_05437 (By similarity). The
CC atrochrysone carboxylic acid is then converted to atrochrysone which is
CC further transformed into emodin anthrone (By similarity). The next step
CC is performed by the anthrone oxygenase CPUR_05434 that catalyzes the
CC oxidation of emodinanthrone to emodin (By similarity). Emodin is
CC further modified to yield monodictyphenone via several steps involving
CC CPUR_05427, CPUR_05428, CPUR_05429 and CPUR_05430 (By similarity). The
CC short chain dehydrogenase/reductase CPUR_05418 then catalyzes the C-5
CC ketoreduction to give the xanthone skeleton of the monomeric units
CC (PubMed:32105084). Ergochromes formation requires further dimerization
CC steps of different xanthone units, probably catalyzed by the cytochrome
CC P450 monooxygenase CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426
CC and CPUR_05431 are unique to Claviceps, thus it is likely that they are
CC involved in further modification of xanthone units or in their
CC dimerization (PubMed:28955461). The yellow ergochromes and the red
CC anthraquinone pigments endocrocin and clavorubin are products from the
CC same PKS derived precursors and the latter are likely shunt products in
CC the pathway of xanthone biosynthesis (PubMed:28955461). It is proposed
CC that atrochrysone carboxylic acid released from the PKS CPUR_05437 can
CC also be converted to endocrocin anthrone which is further oxidized into
CC endocrocin by CPUR_05435 (By similarity). Endocrocin could be then
CC modified to clavorubin, possibly by CPUR_05423 and CPUR_05431
CC (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite
CC produced by the cluster with a much higher yield compared to endocrocin
CC (PubMed:28955461). {ECO:0000250|UniProtKB:Q4W944,
CC ECO:0000250|UniProtKB:Q5BH30, ECO:0000269|PubMed:28955461,
CC ECO:0000269|PubMed:30996871, ECO:0000269|PubMed:32105084}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30394754}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CAGA01000032; CCE31566.1; -; Genomic_DNA.
DR SMR; M1W266; -.
DR EnsemblFungi; CCE31566; CCE31566; CPUR_05419.
DR VEuPathDB; FungiDB:CPUR_05419; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_033574_2_0_1; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; M1W266; -.
DR Proteomes; UP000016801; 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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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..534
FT /note="Cytochrome P450 monooxygenase CPUR_05419"
FT /id="PRO_0000453478"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 473
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 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 534 AA; 59905 MW; 7F0BE2B603B96F80 CRC64;
MTDFKNDTIP DMSWTTGSNS GLLSSSPTTL ALATLATGLA VFLVYLAYTP SVDALAPEFT
SDTTPLIGSW GFYSRRWSFW RDSVARSKTG QFSFWLGKNH VVGVSGAAAR KMFLDHQSLD
RIKAAPLHGI GPEIVPPIHF VHQPNFSKGH SYFQRRVLDL MKTEHLASRL HAATREARTV
FRGFPTKQTT LKGTRSGIVS PVDSCYRLVL SQSVRMMFCD ELVDTHELFE KYVAFTHELQ
HLNSGHTCAV PWLPSLAHTK RRYYRHRLHC LFTPLVEKRL QSQQGRAGSR ANDALQILVD
NGDELDNIVT FLISVLFISI ANAGKLAGVL LNILCQNPIW QDRVLSEINA ATPKFWPADK
PATLVEKLDG MPLEVWEASF PFVELIIREA IRMHVAFPMT RLNVSSRAIP IPGTGQVVPS
GSFAAYNTND AHLNEALYPD PLRFDPERFE TPREGAKTET YGFLGWGNGR HRCVGQRWAK
LQLSINLVYA VAMYKWNSCD ADGNALPPVD HSFDRDRHGN QLAQGVFCKY ECRE
