CUTI1_COLGL
ID CUTI1_COLGL Reviewed; 224 AA.
AC P11373; Q8X1A3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cutinase 1;
DE EC=3.1.1.74 {ECO:0000305|PubMed:17043825};
DE AltName: Full=Cutin hydrolase 1;
DE Flags: Precursor;
GN Name=CUTA;
OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=474922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ettinger W.F., Thukral S.K., Kolattukudy P.E.;
RT "Structure of cutinase gene, cDNA, and the derived amino acid sequence from
RT phytopathogenic fungi.";
RL Biochemistry 26:7883-7892(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Abu Bakar F.D., Cooper D.M., Zamrod Z., Mahadi N.M., Sullivan P.A.;
RT "Cloning and characterization of the cutinase-encoding gene and cDNA from
RT the fungal phytopathogen, Glomerella cingulata.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, INDUCTION, AND BLOCKED N-TERMINUS.
RC STRAIN=Ch27;
RX PubMed=17043825; DOI=10.1007/s00253-006-0605-1;
RA Chen Z., Franco C.F., Baptista R.P., Cabral J.M.S., Coelho A.V.,
RA Rodrigues C.J. Jr., Melo E.P.;
RT "Purification and identification of cutinases from Colletotrichum kahawae
RT and Colletotrichum gloeosporioides.";
RL Appl. Microbiol. Biotechnol. 73:1306-1313(2007).
RN [4] {ECO:0007744|PDB:3DCN, ECO:0007744|PDB:3DD5, ECO:0007744|PDB:3DEA}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 31-224, ACTIVE SITE, DISULFIDE
RP BONDS, AND MUTAGENESIS OF HIS-204.
RX PubMed=18983850; DOI=10.1016/j.jmb.2008.10.050;
RA Nyon M.P., Rice D.W., Berrisford J.M., Hounslow A.M., Moir A.J., Huang H.,
RA Nathan S., Mahadi N.M., Bakar F.D., Craven C.J.;
RT "Catalysis by Glomerella cingulata cutinase requires conformational cycling
RT between the active and inactive states of its catalytic triad.";
RL J. Mol. Biol. 385:226-235(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:17043825). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle
CC (PubMed:17043825). Allows pathogenic fungi to penetrate through the
CC cuticular barrier into the host plant during the initial stage of
CC fungal infection (By similarity). {ECO:0000250|UniProtKB:P00590,
CC ECO:0000269|PubMed:17043825}.
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, ECO:0000305|PubMed:17043825};
CC -!- ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate (DFP).
CC {ECO:0000269|PubMed:17043825}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17043825}.
CC -!- INDUCTION: By contact with cutin. {ECO:0000269|PubMed:17043825}.
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:0000305|Ref.1}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17043825}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined MW is: 20.8 kDa.
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; M21443; AAA33042.1; -; Genomic_DNA.
DR EMBL; AF444194; AAL38030.1; -; Genomic_DNA.
DR PIR; B27451; B27451.
DR PDB; 3DCN; X-ray; 1.90 A; A=31-224.
DR PDB; 3DD5; X-ray; 2.60 A; A/B/C/D/E/F/G/H=31-224.
DR PDB; 3DEA; X-ray; 2.30 A; A/B=31-224.
DR PDBsum; 3DCN; -.
DR PDBsum; 3DD5; -.
DR PDBsum; 3DEA; -.
DR AlphaFoldDB; P11373; -.
DR SMR; P11373; -.
DR ESTHER; colgl-cutas; Cutinase.
DR OMA; KIFCLPT; -.
DR BRENDA; 3.1.1.74; 1569.
DR EvolutionaryTrace; P11373; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0050525; F:cutinase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal;
KW Virulence.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..224
FT /note="Cutinase 1"
FT /id="PRO_0000006437"
FT ACT_SITE 136
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18983850"
FT ACT_SITE 191
FT /evidence="ECO:0000305|PubMed:18983850"
FT ACT_SITE 204
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:18983850"
FT SITE 57
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 137
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 46..125
FT /evidence="ECO:0000269|PubMed:18983850,
FT ECO:0007744|PDB:3DCN, ECO:0007744|PDB:3DD5,
FT ECO:0007744|PDB:3DEA"
FT DISULFID 187..194
FT /evidence="ECO:0000269|PubMed:18983850,
FT ECO:0007744|PDB:3DCN, ECO:0007744|PDB:3DD5,
FT ECO:0007744|PDB:3DEA"
FT MUTAGEN 204
FT /note="H->N: Abolishes substrate binding."
FT /evidence="ECO:0000269|PubMed:18983850"
FT CONFLICT 6..7
FT /note="VL -> IV (in Ref. 2; AAL38030)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="N -> D (in Ref. 2; AAL38030)"
FT /evidence="ECO:0000305"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:3DCN"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3DCN"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3DCN"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:3DCN"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:3DCN"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3DCN"
FT TURN 166..173
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3DCN"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:3DCN"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:3DCN"
SQ SEQUENCE 224 AA; 23477 MW; 1C5BACEAB469ABFA CRC64;
MKFLSVLSLA ITLAAAAPVE VETGVALETR QSSTRNELET GSSSACPKVI YIFARASTEP
GNMGISAGPI VADALERIYG ANNVWVQGVG GPYLADLASN FLPDGTSSAA INEARRLFTL
ANTKCPNAAI VSGGYSQGTA VMAGSISGLS TTIKNQIKGV VLFGYTKNLQ NLGRIPNFET
SKTEVYCDIA DAVCYGTLFI LPAHFLYQTD AAVAAPRFLQ ARIG
