| IED ID | IndEnz0010000320 |
| Enzyme Type ID | esterase000320 |
| Protein Name |
Cutinase 1 EC 3.1.1.74 Cutin hydrolase 1 |
| Gene Name | CUT1 CUTA |
| Organism | Fusarium vanettenii (Neocosmospora pisi) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium solani species complex Fusarium vanettenii (Neocosmospora pisi) |
| Enzyme Sequence | MKFFALTTLLAATASALPTSNPAQELEARQLGRTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGSA |
| Enzyme Length | 230 |
| Uniprot Accession Number | P00590 |
| Absorption | |
| Active Site | ACT_SITE 136; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY"; ACT_SITE 191; /evidence="ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY"; ACT_SITE 204; /note="Proton donor/acceptor"; /evidence="ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by n-undecyl phosphonate (C11Y4) (PubMed:25219509). Inhibited by paraoxon (PubMed:8286366, PubMed:25219509). {ECO:0000269|PubMed:25219509, ECO:0000269|PubMed:8286366}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000269|PubMed:18658138, ECO:0000305|PubMed:19810726, ECO:0000305|PubMed:8286366, ECO:0000305|PubMed:8555209}; |
| DNA Binding | |
| EC Number | 3.1.1.74 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209, ECO:0000269|Ref.4}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is below 30 degrees Celsius (PubMed:19810726). Optimum temperature is 30-40 degrees Celsius (PubMed:18658138). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18658138}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (5); Chain (1); Disulfide bond (2); Helix (11); Modified residue (1); Mutagenesis (7); Propeptide (1); Sequence conflict (2); Signal peptide (1); Site (2); Turn (4) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Secreted;Serine esterase;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}. |
| Modified Residue | MOD_RES 32; /note=N-D-glucuronoyl glycine; /evidence=ECO:0000269|PubMed:7398618 |
| Post Translational Modification | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}.; PTM: O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid. {ECO:0000269|PubMed:7398618}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (46) |
| Cross Reference PDB | 1AGY; 1CEX; 1CUA; 1CUB; 1CUC; 1CUD; 1CUE; 1CUF; 1CUG; 1CUH; 1CUI; 1CUJ; 1CUS; 1CUU; 1CUV; 1CUW; 1CUX; 1CUY; 1CUZ; 1FFA; 1FFB; 1FFC; 1FFD; 1FFE; 1OXM; 1XZA; 1XZB; 1XZC; 1XZD; 1XZE; 1XZF; 1XZG; 1XZH; 1XZI; 1XZJ; 1XZK; 1XZL; 1XZM; 2CUT; 3EF3; 3ESA; 3ESB; 3ESC; 3ESD; 3QPA; 3QPC; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,982 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 uM for p-nitrophenyl acetate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=1.26 uM for p-nitrophenyl butyrate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=0.68 mM for p-nitrophenyl butyrate (at pH 9 and 30 degrees Celsius) {ECO:0000269|PubMed:8555209}; KM=1.48 uM for p-nitrophenyl valerate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=1.50 uM for p-nitrophenyl hexanoate (at pH 7.5) {ECO:0000269|PubMed:19810726}; Note=kcat is 1800 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 9 and 30 degrees Celsius). {ECO:0000269|PubMed:8555209}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.74; |