Summary: Cutinase
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Cutinase Edit Wikipedia article
| Cutinase | |||||||||
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| Identifiers | |||||||||
| Symbol | Cutinase | ||||||||
| Pfam | PF01083 | ||||||||
| InterPro | IPR000675 | ||||||||
| PROSITE | PDOC00140 | ||||||||
| SCOPe | 1cex / SUPFAM | ||||||||
| OPM superfamily | 127 | ||||||||
| OPM protein | 1oxm | ||||||||
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A cutinase (EC 3.1.1.74) is an enzyme that catalyzes the chemical reaction
- cutin + H2O cutin monomers
Thus, the two substrates of this enzyme are cutin and H2O, whereas its product is cutin monomer.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase.
Aerial plant organs are protected by a cuticle composed of an insoluble polymeric structural compound, cutin, which is a polyester composed of hydroxy and hydroxyepoxy fatty acids.[2] Plant pathogenic fungi produce extracellular degradative enzymes[3] that play an important role in pathogenesis. They include cutinase, which hydrolyses cutin, facilitating fungus penetration through the cuticle. Inhibition of the enzyme can prevent fungal infection through intact cuticles. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore, the mechanism for which is as yet unknown.[2][3]
Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases.[2] The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases.[4] The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.[2] Two cutinase-like proteins (MtCY39.35 and MtCY339.08c) have been found in the genome of the bacteria Mycobacterium tuberculosis.
References
- ^ Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C (May 1997). "Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis". J. Mol. Biol. 268 (4): 779–99. doi:10.1006/jmbi.1997.1000. PMID 9175860.
- ^ a b c d Ettinger WF, Thukral SK, Kolattukudy PE (1987). "Structure of cutinase gene, cDNA, and the derived amino acid sequence from phytopathogenic fungi". Biochemistry. 26 (24): 7883–7892. doi:10.1021/bi00398a052.
- ^ a b Sweigard JA, Chumley FG, Valent B (1992). "Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea". Mol. Gen. Genet. 232 (2): 174–182. doi:10.1007/BF00279994. PMID 1557023.
- ^ Cambillau C, Martinez C, De Geus P, Lauwereys M, Matthyssens G (1992). "Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent". Nature. 356 (6370): 615–618. doi:10.1038/356615a0. PMID 1560844.
- Garcia-Lepe R, Nuero OM, Reyes F, Santamaria F (1997). "Lipases in autolysed cultures of filamentous fungi". Lett. Appl. Microbiol. 25 (2): 127–30. doi:10.1046/j.1472-765X.1997.00187.x. PMID 9281862.
- Purdy RE, Kolattukudy PE (1975). "Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi". Biochemistry. 14 (13): 2824–31. doi:10.1021/bi00684a006. PMID 1156575.
- Purdy RE, Kolattukudy PE (1975). "Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi". Biochemistry. 14 (13): 2832–40. doi:10.1021/bi00684a007. PMID 239740.
See also
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Literature references
-
Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C; , J Mol Biol 1997;268:779-799.: Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. PUBMED:9175860 EPMC:9175860
Internal database links
| SCOOP: | Abhydrolase_1 Abhydrolase_2 Abhydrolase_6 Abhydrolase_8 DUF2974 DUF676 Hydrolase_4 Lipase_3 PE-PPE Thioesterase VirJ |
| Similarity to PfamA using HHSearch: | VirJ PE-PPE |
External database links
| CAZY: | CE5 |
| HOMSTRAD: | Cutinase |
| PROSITE: | PDOC00140 |
| SCOP: | 1cex |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000675
Plant pathogenic fungi produce extracellular degradative enzymes [PUBMED:1557023] that play an important role in pathogenesis. They include cutinase, which hydrolyses cutin, facilitating fungus penetration through the cuticle. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases [PUBMED:1560844]. The protein also contains 2 disulphide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.
Acetylxylan esterase removes acetyl side groups from xylan. The catalytic core of the enzyme has an alpha/beta/alpha sandwich fold, similar to that of cutinase [PUBMED:11243887].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | hydrolase activity (GO:0016787) |
Domain organisation
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Pfam Clan
This family is a member of clan AB_hydrolase (CL0028), which has the following description:
This catalytic domain is found in a very wide range of enzymes.
The clan contains the following 70 members:
Abhydro_lipase Abhydrolase_1 Abhydrolase_2 Abhydrolase_3 Abhydrolase_4 Abhydrolase_5 Abhydrolase_6 Abhydrolase_7 Abhydrolase_8 Abhydrolase_9 Acyl_transf_2 Asp2 AXE1 BAAT_C Chlorophyllase Chlorophyllase2 COesterase Cutinase DLH DUF1057 DUF1100 DUF1350 DUF1400 DUF1749 DUF2048 DUF2235 DUF2920 DUF2974 DUF3089 DUF3141 DUF3530 DUF452 DUF676 DUF726 DUF818 DUF829 DUF900 DUF915 EHN Esterase Esterase_PHB FSH1 Hydrolase_4 LCAT LIDHydrolase LIP Lipase Lipase3_N Lipase_2 Lipase_3 Ndr PAE PAF-AH_p_II Palm_thioest PE-PPE Peptidase_S10 Peptidase_S15 Peptidase_S28 Peptidase_S37 Peptidase_S9 PGAP1 PhaC_N PHB_depo_C PhoPQ_related Say1_Mug180 Ser_hydrolase Tannase Thioesterase UPF0227 VirJAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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| Seed (15) |
Full (4192) |
Representative proteomes | UniProt (11775) |
NCBI (17714) |
Meta (2) |
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| RP15 (345) |
RP35 (1351) |
RP55 (2984) |
RP75 (5921) |
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| PP/heatmap | 1 | ||||||||
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| Seed (15) |
Full (4192) |
Representative proteomes | UniProt (11775) |
NCBI (17714) |
Meta (2) |
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|---|---|---|---|---|---|---|---|---|---|
| RP15 (345) |
RP35 (1351) |
RP55 (2984) |
RP75 (5921) |
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| Raw Stockholm | |||||||||
| Gzipped | |||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Sequence Ontology: | SO:0000417 |
| Author: |
Finn RD  , Bateman A
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| Number in seed: | 15 |
| Number in full: | 4192 |
| Average length of the domain: | 185.00 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 66.25 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 178 | ||||||||||||
| Family (HMM) version: | 23 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
CutinaseStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cutinase domain has been found. There are 100 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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