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P00590

- CUTI1_FUSSO

UniProt

P00590 - CUTI1_FUSSO

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Protein

Cutinase 1

Gene

CUT1

Organism
Fusarium solani subsp. pisi (Nectria haematococca)
Status
Reviewed - 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-KW
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 – 414
Helixi44 – 463
Beta strandi49 – 557
Turni62 – 676
Helixi68 – 7912
Turni81 – 833
Beta strandi84 – 885
Helixi97 – 1015
Helixi108 – 12417
Beta strandi129 – 1357
Helixi137 – 14812
Helixi151 – 1544
Beta strandi157 – 1648
Turni166 – 1738
Helixi180 – 1823
Beta strandi183 – 1864
Helixi192 – 1954
Helixi202 – 2054
Helixi208 – 2125
Helixi214 – 22714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
K02640 mRNA. Translation: AAA33334.1.
M29759 Genomic DNA. Translation: AAA33335.1.
PIRiA32836. UVFUS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02640 mRNA. Translation: AAA33334.1 .
M29759 Genomic DNA. Translation: AAA33335.1 .
PIRi A32836. UVFUS.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AGY X-ray 1.15 A 31-230 [» ]
1CEX X-ray 1.00 A 17-230 [» ]
1CUA X-ray 1.80 A 17-230 [» ]
1CUB X-ray 1.75 A 17-230 [» ]
1CUC X-ray 1.75 A 17-230 [» ]
1CUD X-ray 2.70 A/B/C 17-230 [» ]
1CUE X-ray 2.10 A 33-229 [» ]
1CUF X-ray 1.75 A 17-230 [» ]
1CUG X-ray 1.75 A 17-230 [» ]
1CUH X-ray 1.75 A 17-230 [» ]
1CUI X-ray 2.50 A 17-230 [» ]
1CUJ X-ray 1.60 A 17-230 [» ]
1CUS X-ray 1.25 A 31-230 [» ]
1CUU X-ray 1.69 A 17-230 [» ]
1CUV X-ray 2.01 A 17-230 [» ]
1CUW X-ray 2.70 A/B 17-230 [» ]
1CUX X-ray 1.75 A 17-230 [» ]
1CUY X-ray 1.69 A 17-230 [» ]
1CUZ X-ray 2.10 A 17-230 [» ]
1FFA X-ray 1.69 A 17-230 [» ]
1FFB X-ray 1.75 A 17-230 [» ]
1FFC X-ray 1.75 A 17-230 [» ]
1FFD X-ray 1.69 A 17-230 [» ]
1FFE X-ray 1.69 A 17-230 [» ]
1OXM X-ray 2.30 A/B 17-230 [» ]
1XZA X-ray 1.80 A 17-230 [» ]
1XZB X-ray 1.75 A 17-230 [» ]
1XZC X-ray 1.75 A 17-230 [» ]
1XZD X-ray 2.70 A 17-228 [» ]
1XZE X-ray 1.75 A 17-230 [» ]
1XZF X-ray 1.69 A 17-230 [» ]
1XZG X-ray 1.69 A 17-230 [» ]
1XZH X-ray 1.69 A 17-230 [» ]
1XZI X-ray 1.69 A 17-230 [» ]
1XZJ X-ray 1.69 A 17-230 [» ]
1XZK X-ray 2.01 A/B 17-230 [» ]
1XZL X-ray 1.69 A 17-230 [» ]
1XZM X-ray 1.75 A 17-230 [» ]
2CUT X-ray 1.90 A 31-228 [» ]
3EF3 X-ray 1.50 A 17-230 [» ]
3ESA X-ray 2.00 A/B 17-230 [» ]
3ESB X-ray 2.30 A 17-230 [» ]
3ESC X-ray 1.20 A 17-230 [» ]
3ESD X-ray 1.22 A 17-230 [» ]
3QPA X-ray 0.85 A 32-228 [» ]
3QPC X-ray 0.98 A 32-228 [» ]
ProteinModelPortali P00590.
SMRi P00590. Positions 33-229.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2176862.

PTM databases

UniCarbKBi P00590.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.1.1.74. 9402.

Miscellaneous databases

EvolutionaryTracei P00590.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000675. Cutinase.
IPR011150. Cutinase_monf.
[Graphical view ]
Pfami PF01083. Cutinase. 1 hit.
[Graphical view ]
PRINTSi PR00129. CUTINASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 110 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