PIG14_CLAP2
ID PIG14_CLAP2 Reviewed; 310 AA.
AC M1WCF7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Atrochrysone carboxyl ACP thioesterase CPUR_05436 {ECO:0000303|PubMed:28955461};
DE EC=3.1.2.- {ECO:0000305|PubMed:28955461};
DE AltName: Full=Ergochrome gene cluster protein CPUR_05436 {ECO:0000303|PubMed:28955461};
GN ORFNames=CPUR_05436;
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, AND INDUCTION.
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 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: Atrochrysone carboxyl ACP thioesterase; part of the
CC ergochrome gene cluster responsible for the typical purple-black color
CC of the ergot sclerotia (PubMed:28955461). The ergochrome gene cluster
CC 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:Q4W945,
CC ECO:0000250|UniProtKB:Q5BH30, ECO:0000269|PubMed:28955461,
CC ECO:0000269|PubMed:32105084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate +
CC H(+) + holo-[ACP]; Xref=Rhea:RHEA:64236, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:149712, ChEBI:CHEBI:149713;
CC Evidence={ECO:0000305|PubMed:28955461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000305|PubMed:28955461};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q988B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q988B9};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:28955461}.
CC -!- INDUCTION: Expression starts 10 days after infection and shows an
CC increase towards the late stages of infection which correlates with the
CC formation of the sclerotia and thus the pigment production
CC (PubMed:28955461). Is directly regulated by the cluster-specific
CC activator CPUR_05433 (PubMed:28955461). {ECO:0000269|PubMed:28955461}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; CAGA01000032; CCE31583.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WCF7; -.
DR SMR; M1WCF7; -.
DR STRING; 1111077.M1WCF7; -.
DR EnsemblFungi; CCE31583; CCE31583; CPUR_05436.
DR VEuPathDB; FungiDB:CPUR_05436; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR OrthoDB; 576967at2759; -.
DR PhylomeDB; M1WCF7; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..310
FT /note="Atrochrysone carboxyl ACP thioesterase CPUR_05436"
FT /id="PRO_0000443985"
FT ACT_SITE 109
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ SEQUENCE 310 AA; 34761 MW; A4608A98DC0BCA3E CRC64;
MAGDKGGYRQ INSSLNICAF EDYLKSQTDN LPELPDVEQI TPRVLRVLGQ NPGKFTYQGT
NTYIVGTGKH RLIVDTSGGE IEWAELLEST LSSLNISLSH VLLTHWHGDH TGGVPDLLRI
YPHLEHDIYK NEPESGQQDI VDGQIFRVEG ATVRALHVPG HSDDHMCFIL EEEQAMFTGD
NILGHGTSAV EDLGTFMASM QRMLDQRCLT GYSAHGAVIA DLPGKIRTEL ANKRRREKQI
LLALGRVRQR RQKSITVEDL VTEIYGESMD ESTRTLALTP FTDEVLRKLA GDFKVAFEVR
AGKRRWYSVE
