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P00590 (CUTI1_FUSSO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cutinase 1

EC=3.1.1.74
Alternative name(s):
Cutin hydrolase 1
Gene names
Name:CUT1
Synonyms:CUTA
OrganismFusarium solani subsp. pisi (Nectria haematococca)
Taxonomic identifier70791 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium solani species complex

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Cutin + H2O = cutin monomers.

Subcellular location

Secreted.

Induction

By contact with cutin.

Post-translational modification

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.

O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid. Ref.3

Sequence similarities

Belongs to the cutinase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncutinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 230199Cutinase 1
PRO_0000006440

Sites

Active site1361
Active site1911
Active site2041

Amino acid modifications

Modified residue321N-D-glucuronoyl glycine Ref.3
Disulfide bond47 ↔ 194
Disulfide bond125 ↔ 187

Experimental info

Sequence conflict481R → A in AAA33335. Ref.2
Sequence conflict941R → A in AAA33335. Ref.2

Secondary structure

...................................... 230
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00590 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7253ACAA657AD1AB

FASTA23023,982
        10         20         30         40         50         60 
MKFFALTTLL AATASALPTS NPAQELEARQ LGRTTRDDLI NGNSASCRDV IFIYARGSTE 

        70         80         90        100        110        120 
TGNLGTLGPS IASNLESAFG KDGVWIQGVG GAYRATLGDN ALPRGTSSAA IREMLGLFQQ 

       130        140        150        160        170        180 
ANTKCPDATL IAGGYSQGAA LAAASIEDLD SAIRDKIAGT VLFGYTKNLQ NRGRIPNYPA 

       190        200        210        220        230 
DRTKVFCNTG DLVCTGSLIV AAPHLAYGPD ARGPAPEFLI EKVRAVRGSA 

« Hide

References

[1]"Cloning and structure determination of cDNA for cutinase, an enzyme involved in fungal penetration of plants."
Soliday C.L., Flurkey W.H., Okita T.W., Kolattukudy P.E.
Proc. Natl. Acad. Sci. U.S.A. 81:3939-3943(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-94; 113-142 AND 183-192.
Strain: T-8.
[2]"Structure of the cutinase gene and detection of promoter activity in the 5'-flanking region by fungal transformation."
Soliday C.L., Dickman M.B., Kolattukudy P.E.
J. Bacteriol. 171:1942-1951(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus."
Lin T.-S., Kolattukudy P.E.
Eur. J. Biochem. 106:341-351(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: GLUCURONIC-ACID BINDING AT GLY-32, GLYCOSYLATION.
[4]"Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent."
Martinez C., de Geus P., Lauwereys M., Matthyssens G., Cambillau C.
Nature 356:615-618(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[5]"Cutinase, a lipolytic enzyme with a preformed oxyanion hole."
Martinez C., Nicolas A., van Tilbeurgh H., Egloff M.-P., Cudrey C., Verger R., Cambillau C.
Biochemistry 33:83-89(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]"Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis."
Longhi S., Czjzek M., Lamzin V., Nicolas A., Cambillau C.
J. Mol. Biol. 268:779-799(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 17-230.
[7]Nicolas A., Martinez C., Cambillau C.
Submitted (MAR-1997) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 33-230.
[8]"1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution."
Prompers J.J., Groenewegen A., van Schaik R.C., Pepermans H.A.M., Hilbers C.W.
Protein Sci. 6:2375-2384(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02640 mRNA. Translation: AAA33334.1.
M29759 Genomic DNA. Translation: AAA33335.1.
PIRUVFUS. A32836.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGYX-ray1.15A31-230[»]
1CEXX-ray1.00A17-230[»]
1CUAX-ray1.80A17-230[»]
1CUBX-ray1.75A17-230[»]
1CUCX-ray1.75A17-230[»]
1CUDX-ray2.70A/B/C17-230[»]
1CUEX-ray2.10A33-229[»]
1CUFX-ray1.75A17-230[»]
1CUGX-ray1.75A17-230[»]
1CUHX-ray1.75A17-230[»]
1CUIX-ray2.50A17-230[»]
1CUJX-ray1.60A17-230[»]
1CUSX-ray1.25A31-230[»]
1CUUX-ray1.69A17-230[»]
1CUVX-ray2.01A17-230[»]
1CUWX-ray2.70A/B17-230[»]
1CUXX-ray1.75A17-230[»]
1CUYX-ray1.69A17-230[»]
1CUZX-ray2.10A17-230[»]
1FFAX-ray1.69A17-230[»]
1FFBX-ray1.75A17-230[»]
1FFCX-ray1.75A17-230[»]
1FFDX-ray1.69A17-230[»]
1FFEX-ray1.69A17-230[»]
1OXMX-ray2.30A/B17-230[»]
1XZAX-ray1.80A17-230[»]
1XZBX-ray1.75A17-230[»]
1XZCX-ray1.75A17-230[»]
1XZDX-ray2.70A17-228[»]
1XZEX-ray1.75A17-230[»]
1XZFX-ray1.69A17-230[»]
1XZGX-ray1.69A17-230[»]
1XZHX-ray1.69A17-230[»]
1XZIX-ray1.69A17-230[»]
1XZJX-ray1.69A17-230[»]
1XZKX-ray2.01A/B17-230[»]
1XZLX-ray1.69A17-230[»]
1XZMX-ray1.75A17-230[»]
2CUTX-ray1.90A31-228[»]
3EF3X-ray1.50A17-230[»]
3ESAX-ray2.00A/B17-230[»]
3ESBX-ray2.30A17-230[»]
3ESCX-ray1.20A17-230[»]
3ESDX-ray1.22A17-230[»]
3QPAX-ray0.85A32-228[»]
3QPCX-ray0.98A32-228[»]
ProteinModelPortalP00590.
SMRP00590. Positions 33-229.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2176862.

PTM databases

UniCarbKBP00590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.74. 9402.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000675. Cutinase.
IPR011150. Cutinase_monf.
[Graphical view]
PfamPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSPR00129. CUTINASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00590.

Entry information

Entry nameCUTI1_FUSSO
AccessionPrimary (citable) accession number: P00590
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references