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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei136 – 1361By similarity
Active sitei191 – 1911By similarity
Active sitei204 – 2041By similarity

GO - Molecular functioni

  • cutinase activity Source: UniProtKB

GO - Biological processi

  • 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 224208Cutinase 1PRO_0000006437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni37 – 393Combined sources
Beta strandi48 – 547Combined sources
Turni61 – 633Combined sources
Helixi67 – 7913Combined sources
Helixi81 – 833Combined sources
Beta strandi84 – 885Combined sources
Helixi98 – 1014Combined sources
Helixi108 – 12417Combined sources
Beta strandi128 – 1358Combined sources
Helixi137 – 14610Combined sources
Helixi151 – 1566Combined sources
Beta strandi157 – 1637Combined sources
Turni166 – 1738Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1864Combined sources
Helixi192 – 1954Combined sources
Helixi208 – 2125Combined sources
Helixi214 – 2207Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 33-224.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72VL → IV in AAL38030 (Ref. 2) Curated
Sequence conflicti83 – 831N → D in AAL38030 (Ref. 2) Curated

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
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. Positions 33-224.
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...

Publicationsi

  1. "Structure of cutinase gene, cDNA, and the derived amino acid sequence from phytopathogenic fungi."
    Ettinger W.F., Thukral S.K., Kolattukudy P.E.
    Biochemistry 26:7883-7892(1987)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and characterization of the cutinase-encoding gene and cDNA from the fungal phytopathogen, Glomerella cingulata."
    Abu Bakar F.D., Cooper D.M., Zamrod Z., Mahadi N.M., Sullivan P.A.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Purification and identification of cutinases from Colletotrichum kahawae and Colletotrichum gloeosporioides."
    Chen Z., Franco C.F., Baptista R.P., Cabral J.M.S., Coelho A.V., Rodrigues C.J. Jr., Melo E.P.
    Appl. Microbiol. Biotechnol. 73:1306-1313(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION, BLOCKED N-TERMINUS.
    Strain: Ch27.

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: May 11, 2016
This is version 79 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.