Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cutinase 1

Gene

CUTA

Organism
Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.1 Publication

Catalytic activityi

Cutin + H2O = cutin monomers.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Inhibited by diisopropylfluorophosphate (DFP).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei136By similarity1
Active sitei191By similarity1
Active sitei204By similarity1

GO - Molecular functioni

  • cutinase activity Source: UniProtKB

GO - Biological processi

  • metabolic process Source: InterPro
  • pathogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERicolgl-cutas. Cutinase.

Names & Taxonomyi

Protein namesi
Recommended name:
Cutinase 1 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 1
Gene namesi
Name:CUTA
OrganismiColletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata)
Taxonomic identifieri474922 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeGlomerellalesGlomerellaceaeColletotrichum

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000000643717 – 224Cutinase 1Add BLAST208

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 194By similarity
Disulfide bondi125 ↔ 187By similarity

Post-translational modificationi

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.
The N-terminus is blocked.

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By contact with cutin.1 Publication

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni37 – 39Combined sources3
Beta strandi48 – 54Combined sources7
Turni61 – 63Combined sources3
Helixi67 – 79Combined sources13
Helixi81 – 83Combined sources3
Beta strandi84 – 88Combined sources5
Helixi98 – 101Combined sources4
Helixi108 – 124Combined sources17
Beta strandi128 – 135Combined sources8
Helixi137 – 146Combined sources10
Helixi151 – 156Combined sources6
Beta strandi157 – 163Combined sources7
Turni166 – 173Combined sources8
Helixi180 – 182Combined sources3
Beta strandi183 – 186Combined sources4
Helixi192 – 195Combined sources4
Helixi208 – 212Combined sources5
Helixi214 – 220Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DCNX-ray1.90A31-224[»]
3DD5X-ray2.60A/B/C/D/E/F/G/H31-224[»]
3DEAX-ray2.30A/B31-224[»]
ProteinModelPortaliP11373.
SMRiP11373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11373.

Family & Domainsi

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase/axe.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLSVLSLA ITLAAAAPVE VETGVALETR QSSTRNELET GSSSACPKVI
60 70 80 90 100
YIFARASTEP GNMGISAGPI VADALERIYG ANNVWVQGVG GPYLADLASN
110 120 130 140 150
FLPDGTSSAA INEARRLFTL ANTKCPNAAI VSGGYSQGTA VMAGSISGLS
160 170 180 190 200
TTIKNQIKGV VLFGYTKNLQ NLGRIPNFET SKTEVYCDIA DAVCYGTLFI
210 220
LPAHFLYQTD AAVAAPRFLQ ARIG
Length:224
Mass (Da):23,477
Last modified:July 1, 1989 - v1
Checksum:i1C5BACEAB469ABFA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6 – 7VL → IV in AAL38030 (Ref. 2) Curated2
Sequence conflicti83N → D in AAL38030 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21443 Genomic DNA. Translation: AAA33042.1.
AF444194 Genomic DNA. Translation: AAL38030.1.
PIRiB27451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21443 Genomic DNA. Translation: AAA33042.1.
AF444194 Genomic DNA. Translation: AAL38030.1.
PIRiB27451.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DCNX-ray1.90A31-224[»]
3DD5X-ray2.60A/B/C/D/E/F/G/H31-224[»]
3DEAX-ray2.30A/B31-224[»]
ProteinModelPortaliP11373.
SMRiP11373.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERicolgl-cutas. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11373.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase/axe.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCUTI1_COLGL
AccessioniPrimary (citable) accession number: P11373
Secondary accession number(s): Q8X1A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

On the 2D-gel the determined MW is: 20.8 kDa.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.