EASC_CLAPU
ID EASC_CLAPU Reviewed; 473 AA.
AC Q6ZXC2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Catalase easC {ECO:0000303|PubMed:21409592};
DE EC=1.11.-.- {ECO:0000305|PubMed:15904941};
DE AltName: Full=Catalase 2 {ECO:0000303|PubMed:11778866};
DE AltName: Full=Ergot alkaloid synthesis protein C {ECO:0000303|PubMed:21409592};
GN Name=easC {ECO:0000303|PubMed:21409592};
GN Synonyms=cpcat2 {ECO:0000303|PubMed:11778866};
OS Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=5111;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOTECHNOLOGY.
RC STRAIN=P1 / 1029/N5;
RX PubMed=11778866; DOI=10.1007/s002530100801;
RA Tudzynski P., Correia T., Keller U.;
RT "Biotechnology and genetics of ergot alkaloids.";
RL Appl. Microbiol. Biotechnol. 57:593-605(2001).
RN [2]
RP FUNCTION.
RX PubMed=14700635; DOI=10.1016/j.chembiol.2003.11.013;
RA Correia T., Grammel N., Ortel I., Keller U., Tudzynski P.;
RT "Molecular cloning and analysis of the ergopeptine assembly system in the
RT ergot fungus Claviceps purpurea.";
RL Chem. Biol. 10:1281-1292(2003).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 20102 / Farmitalia FI 32/17;
RX PubMed=14732265; DOI=10.1016/j.fgb.2003.10.002;
RA Wang J., Machado C., Panaccione D.G., Tsai H.-F., Schardl C.L.;
RT "The determinant step in ergot alkaloid biosynthesis by an endophyte of
RT perennial ryegrass.";
RL Fungal Genet. Biol. 41:189-198(2004).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE EAS CLUSTER.
RX PubMed=15904941; DOI=10.1016/j.phytochem.2005.04.011;
RA Haarmann T., Machado C., Lubbe Y., Correia T., Schardl C.L.,
RA Panaccione D.G., Tudzynski P.;
RT "The ergot alkaloid gene cluster in Claviceps purpurea: extension of the
RT cluster sequence and intra species evolution.";
RL Phytochemistry 66:1312-1320(2005).
RN [5]
RP FUNCTION.
RC STRAIN=P1 / 1029/N5;
RX PubMed=16538694; DOI=10.1002/cbic.200500487;
RA Haarmann T., Ortel I., Tudzynski P., Keller U.;
RT "Identification of the cytochrome P450 monooxygenase that bridges the
RT clavine and ergoline alkaloid pathways.";
RL ChemBioChem 7:645-652(2006).
RN [6]
RP FUNCTION.
RX PubMed=17308187; DOI=10.1128/aem.00257-07;
RA Fleetwood D.J., Scott B., Lane G.A., Tanaka A., Johnson R.D.;
RT "A complex ergovaline gene cluster in epichloe endophytes of grasses.";
RL Appl. Environ. Microbiol. 73:2571-2579(2007).
RN [7]
RP FUNCTION.
RX PubMed=17720822; DOI=10.1128/aem.01040-07;
RA Lorenz N., Wilson E.V., Machado C., Schardl C.L., Tudzynski P.;
RT "Comparison of ergot alkaloid biosynthesis gene clusters in Claviceps
RT species indicates loss of late pathway steps in evolution of C.
RT fusiformis.";
RL Appl. Environ. Microbiol. 73:7185-7191(2007).
RN [8]
RP FUNCTION.
RX PubMed=17560817; DOI=10.1016/j.fgb.2007.04.008;
RA Haarmann T., Lorenz N., Tudzynski P.;
RT "Use of a nonhomologous end joining deficient strain (Deltaku70) of the
RT ergot fungus Claviceps purpurea for identification of a nonribosomal
RT peptide synthetase gene involved in ergotamine biosynthesis.";
RL Fungal Genet. Biol. 45:35-44(2008).
RN [9]
RP FUNCTION.
RX PubMed=19139103; DOI=10.1074/jbc.m807168200;
RA Ortel I., Keller U.;
RT "Combinatorial assembly of simple and complex D-lysergic acid alkaloid
RT peptide classes in the ergot fungus Claviceps purpurea.";
RL J. Biol. Chem. 284:6650-6660(2009).
RN [10]
RP FUNCTION.
RX PubMed=20118373; DOI=10.1128/aem.00737-09;
RA Lorenz N., Olsovska J., Sulc M., Tudzynski P.;
RT "Alkaloid cluster gene ccsA of the ergot fungus Claviceps purpurea encodes
RT chanoclavine I synthase, a flavin adenine dinucleotide-containing
RT oxidoreductase mediating the transformation of N-methyl-
RT dimethylallyltryptophan to chanoclavine I.";
RL Appl. Environ. Microbiol. 76:1822-1830(2010).
RN [11]
RP FUNCTION.
RC STRAIN=ATCC 20102 / Farmitalia FI 32/17;
RX PubMed=20735127; DOI=10.1021/ja105785p;
RA Cheng J.Z., Coyle C.M., Panaccione D.G., O'Connor S.E.;
RT "Controlling a structural branch point in ergot alkaloid biosynthesis.";
RL J. Am. Chem. Soc. 132:12835-12837(2010).
RN [12]
RP FUNCTION.
RX PubMed=21409592; DOI=10.1007/s00294-011-0336-4;
RA Goetz K.E., Coyle C.M., Cheng J.Z., O'Connor S.E., Panaccione D.G.;
RT "Ergot cluster-encoded catalase is required for synthesis of chanoclavine-I
RT in Aspergillus fumigatus.";
RL Curr. Genet. 57:201-211(2011).
RN [13]
RP FUNCTION.
RX PubMed=21494745; DOI=10.1039/c0ob01215g;
RA Matuschek M., Wallwey C., Xie X., Li S.M.;
RT "New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an
RT agroclavine synthase EasG catalyses, via a non-enzymatic adduct with
RT reduced glutathione, the conversion of chanoclavine-I aldehyde to
RT agroclavine.";
RL Org. Biomol. Chem. 9:4328-4335(2011).
RN [14]
RP FUNCTION.
RX PubMed=24361048; DOI=10.1016/j.chembiol.2013.11.008;
RA Havemann J., Vogel D., Loll B., Keller U.;
RT "Cyclolization of D-lysergic acid alkaloid peptides.";
RL Chem. Biol. 21:146-155(2014).
CC -!- FUNCTION: Catalase; part of the gene cluster that mediates the
CC biosynthesis of fungal ergot alkaloid (PubMed:14732265,
CC PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822).
CC DmaW catalyzes the first step of ergot alkaloid biosynthesis by
CC condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-
CC dimethylallyl-L-tryptophan (PubMed:14732265). The second step is
CC catalyzed by the methyltransferase easF that methylates 4-
CC dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine,
CC resulting in the formation of 4-dimethylallyl-L-abrine (By similarity).
CC The catalase easC and the FAD-dependent oxidoreductase easE then
CC transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further
CC oxidized by easD in the presence of NAD(+), resulting in the formation
CC of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592).
CC Agroclavine dehydrogenase easG then mediates the conversion of
CC chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct
CC reaction: the substrate is an iminium intermediate that is formed
CC spontaneously from chanoclavine-I aldehyde in the presence of
CC glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is
CC not required to complete this reaction (PubMed:21494745). Further
CC conversion of agroclavine to paspalic acid is a two-step process
CC involving oxidation of agroclavine to elymoclavine and of elymoclavine
CC to paspalic acid, the second step being performed by the elymoclavine
CC oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then
CC further converted to D-lysergic acid (PubMed:15904941). Ergopeptines
CC are assembled from D-lysergic acid and three different amino acids by
CC the D-lysergyl-peptide-synthetases composed each of a monomudular and a
CC trimodular nonribosomal peptide synthetase subunit (PubMed:14700635,
CC PubMed:15904941). LpsB and lpsC encode the monomodular subunits
CC responsible for D-lysergic acid activation and incorporation into the
CC ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode
CC the trimodular nonribosomal peptide synthetase assembling the
CC tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is
CC responsible for formation of the major ergopeptine, ergotamine, and
CC lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total
CC alkaloid mixture elaborated by C.purpurea (PubMed:17560817,
CC PubMed:19139103). D-lysergyl-tripeptides are assembled by the
CC nonribosomal peptide synthetases and released as N-(D-lysergyl-
CC aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-
CC tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent
CC dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-
CC aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by
CC spontaneous condensation with the terminal lactam carbonyl group
CC (PubMed:24361048). {ECO:0000250|UniProtKB:Q50EL0,
CC ECO:0000269|PubMed:14700635, ECO:0000269|PubMed:14732265,
CC ECO:0000269|PubMed:15904941, ECO:0000269|PubMed:16538694,
CC ECO:0000269|PubMed:17560817, ECO:0000269|PubMed:19139103,
CC ECO:0000269|PubMed:20118373, ECO:0000269|PubMed:20735127,
CC ECO:0000269|PubMed:21409592, ECO:0000269|PubMed:21494745,
CC ECO:0000269|PubMed:24361048, ECO:0000305|PubMed:17308187,
CC ECO:0000305|PubMed:17720822}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P15202};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:15904941}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AJ703808; CAG28311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6ZXC2; -.
DR SMR; Q6ZXC2; -.
DR VEuPathDB; FungiDB:CPUR_04081; -.
DR UniPathway; UPA00327; -.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 1.
DR Pfam; PF00199; Catalase; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase.
FT CHAIN 1..473
FT /note="Catalase easC"
FT /id="PRO_0000439121"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /evidence="ECO:0000250|UniProtKB:P15202"
FT BINDING 344
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:P15202"
SQ SEQUENCE 473 AA; 53629 MW; FCBA47F8B88D9CA0 CRC64;
MASEVSVASS GSEHSGAQKC PFQDPGLSSM DQDSRLRDIL SRFNREKIPE RAVHARGAGA
YGEFEVTHDV SDICDIDMLL GVGKKTPCVV RFSTTTLERG SAESVRDVKG MAIKHFTQDG
NWDWVCLNIP MFFIRDPSKF PDMVHAQRPD PTTNVANPSR WWEFVCNNHE TLHMVMFQFS
DFGTMFDYRS MSGYAAHAYK WVMPDGSWKY VHWFLASDQG PNFETGHQAK QIGADDAESA
TRDLYQSLER GEYPSWTVKV QVVDPEDAPK LPFNILDVTK HWNLGNYPPD IDVIPGRTLG
KLTLKKEPQD YFEEIEQLAF SPSRLVHGVE ASEDPMLQAR LFAYPDAQKH RLGPNNLDLP
ANRTKKFADG ARPEKAEMAP QKVPSQEHAD WVSQVKSSSW SEPNETDYKF PREFWKALPR
LRGEAFQNSL VVNMAKSVSQ VPVDMREKVY STLALIADDL ADRVRTMTEE IVE
