Cutinase
SMART ACC:	SM001110
Description:	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. Plant pathogenic fungi produce extracellular degradative enzymes 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 process is as yet unknown. (PMID 1557023)
InterPro ACC:	IPR000675
InterPro abstract:	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. … expand 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 α-β class, with a central β-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. In the actinobacteria Kineococcus radiotolerans, this enzyme shows a C-terminal extension that is similar to the substrate binding domain of poly(hydroxybutyrate) (PHB) depolymerases [ PUBMED:34705546 ]. Acetylxylan esterase from fungi removes acetyl side groups from xylan. The catalytic core of the enzyme has an α/β/α-sandwich fold, similar to that of cutinase [ PUBMED:11243887 ]. This protein family also includes enzymes that do not show cutinase activity but exhibit esterase activity, such as phospholipases and carboxylesterases from Actinobacteria. Phospholipase Culp4 from Mycobacterium tuberculosis hydrolyses dipalmitoylphosphatidylcholine [ PUBMED:19225166 PUBMED:20103719 ], while Carboxylesterase Culp1 from Mycobacterium tuberculosis hydrolyses various p-nitrophenol-linked aliphatic esters and has weak lipase activity [ PUBMED:19225166 PUBMED:20103719 PUBMED:23843969 ]. collapse
GO function:	hydrolase activity (GO:0016787)
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 7 882 Cutinase domains in 7 877 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing Cutinase domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Cutinase domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Predicted cellular role

Cellular role:	Interaction (with the environment)

Relevant references for this domain

Primary literature for the Cutinase domain is listed below. Automatically-derived, secondary literature is also available.

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a Cutinase domain which could be assigned to a KEGG orthologous group, and not all proteins containing Cutinase domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

InterPro	IPR000675
Pfam	Cutinase