CUTI1_MAGO7
ID CUTI1_MAGO7 Reviewed; 228 AA.
AC P30272; A4QQQ3; G4NG02;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cutinase CUT1 {ECO:0000303|PubMed:1557023};
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Cutin hydrolase;
DE Flags: Precursor;
GN Name=CUT1 {ECO:0000303|PubMed:1557023}; ORFNames=MGG_01943;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4091-5-8;
RX PubMed=1557023; DOI=10.1007/bf00279994;
RA Sweigard J.A., Chumley F.G., Valent B.;
RT "Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea.";
RL Mol. Gen. Genet. 232:174-182(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (By similarity). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle (By
CC similarity). Required for efficient penetration of the host plant
CC cuticle by the appressorium during the initial stage of fungal
CC infection (By similarity). {ECO:0000250|UniProtKB:G4MZV6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-
CC ProRule:PRU10109};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC -!- PTM: The 2 disulfide bonds play a critical role in holding the
CC catalytic residues in juxta-position; reduction of the disulfide
CC bridges results in the complete inactivation of the enzyme.
CC {ECO:0000250|UniProtKB:P11373}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61500; CAA43717.1; -; Genomic_DNA.
DR EMBL; CM001236; EHA46959.1; -; Genomic_DNA.
DR PIR; S20448; S20448.
DR RefSeq; XP_003719326.1; XM_003719278.1.
DR AlphaFoldDB; P30272; -.
DR SMR; P30272; -.
DR ESTHER; maggr-cutas; Cutinase.
DR EnsemblFungi; MGG_01943T0; MGG_01943T0; MGG_01943.
DR GeneID; 2681158; -.
DR KEGG; mgr:MGG_01943; -.
DR VEuPathDB; FungiDB:MGG_01943; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR InParanoid; P30272; -.
DR OMA; KIFCLPT; -.
DR OrthoDB; 1227171at2759; -.
DR BRENDA; 3.1.1.74; 3152.
DR Proteomes; UP000009058; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR InterPro; IPR043580; CUTINASE_1.
DR InterPro; IPR043579; CUTINASE_2.
DR InterPro; IPR011150; Cutinase_monf.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR PRINTS; PR00129; CUTINASE.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00155; CUTINASE_1; 1.
DR PROSITE; PS00931; CUTINASE_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Serine esterase; Signal; Virulence.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..228
FT /note="Cutinase CUT1"
FT /id="PRO_0000006443"
FT ACT_SITE 138
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 193
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 206
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 60
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 139
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..127
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 189..196
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT VARIANT 77
FT /note="A -> R (in strain: 4091-5-8)"
SQ SEQUENCE 228 AA; 24192 MW; 36BF2F253B8F7709 CRC64;
MQFITVALTL IALASASPIA TNVEKPSELE ARQLNSVRND LISGNAAACP SVILIFARAS
GEVGNMGLSA GTNVASALER EFRNDIWVQG VGDPYDAALS PNFLPAGTTQ GAIDEAKRMF
TLANTKCPNA AVVAGGYSQG TAVMFNAVSE MPAAVQDQIK GVVLFGYTKN LQNRGRIPDF
PTEKTEVYCN ASDAVCFGTL FLLPAHFLYT TESSIAAPNW LIRQIRAA
