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Protein

Cutinase 1

Gene

CUT1

Organism
Fusarium solani subsp. pisi (Nectria haematococca)
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.

Catalytic activityi

Cutin + H2O = cutin monomers.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei136 – 1361
Active sitei191 – 1911
Active sitei204 – 2041

GO - Molecular functioni

  1. cutinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.74. 9402.

Names & Taxonomyi

Protein namesi
Recommended name:
Cutinase 1 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 1
Gene namesi
Name:CUT1
Synonyms:CUTA
OrganismiFusarium solani subsp. pisi (Nectria haematococca)
Taxonomic identifieri70791 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium solani species complex

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 230199Cutinase 1PRO_0000006440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321N-D-glucuronoyl glycine1 Publication
Disulfide bondi47 ↔ 194
Disulfide bondi125 ↔ 187

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.
O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP00590.

Expressioni

Inductioni

By contact with cutin.

Structurei

Secondary structure

1
230
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni38 – 414Combined sources
Helixi44 – 463Combined sources
Beta strandi49 – 557Combined sources
Turni62 – 676Combined sources
Helixi68 – 7912Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 885Combined sources
Helixi97 – 1015Combined sources
Helixi108 – 12417Combined sources
Beta strandi129 – 1357Combined sources
Helixi137 – 14812Combined sources
Helixi151 – 1544Combined sources
Beta strandi157 – 1648Combined sources
Turni166 – 1738Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1864Combined sources
Helixi192 – 1954Combined sources
Helixi202 – 2054Combined sources
Helixi208 – 2125Combined sources
Helixi214 – 22714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00590.
SMRiP00590. Positions 33-229.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00590.

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.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
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.

P00590-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFFALTTLL AATASALPTS NPAQELEARQ LGRTTRDDLI NGNSASCRDV
60 70 80 90 100
IFIYARGSTE TGNLGTLGPS IASNLESAFG KDGVWIQGVG GAYRATLGDN
110 120 130 140 150
ALPRGTSSAA IREMLGLFQQ ANTKCPDATL IAGGYSQGAA LAAASIEDLD
160 170 180 190 200
SAIRDKIAGT VLFGYTKNLQ NRGRIPNYPA DRTKVFCNTG DLVCTGSLIV
210 220 230
AAPHLAYGPD ARGPAPEFLI EKVRAVRGSA
Length:230
Mass (Da):23,982
Last modified:July 21, 1986 - v1
Checksum:i7253ACAA657AD1AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481R → A in AAA33335. (PubMed:2703464)Curated
Sequence conflicti94 – 941R → A in AAA33335. (PubMed:2703464)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02640 mRNA. Translation: AAA33334.1.
M29759 Genomic DNA. Translation: AAA33335.1.
PIRiA32836. UVFUS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02640 mRNA. Translation: AAA33334.1.
M29759 Genomic DNA. Translation: AAA33335.1.
PIRiA32836. UVFUS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00590.
SMRiP00590. Positions 33-229.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2176862.

PTM databases

UniCarbKBiP00590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.74. 9402.

Miscellaneous databases

EvolutionaryTraceiP00590.

Family and domain databases

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

Publicationsi

  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. 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.

Entry informationi

Entry nameiCUTI1_FUSSO
AccessioniPrimary (citable) accession number: P00590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

External Data

Dasty 3

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 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.