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P00590

- CUTI1_FUSSO

UniProt

P00590 - CUTI1_FUSSO

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
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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

    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

    MKFFALTTLL AATASALPTS NPAQELEARQ LGRTTRDDLI NGNSASCRDV    50
    IFIYARGSTE TGNLGTLGPS IASNLESAFG KDGVWIQGVG GAYRATLGDN 100
    ALPRGTSSAA IREMLGLFQQ ANTKCPDATL IAGGYSQGAA LAAASIEDLD 150
    SAIRDKIAGT VLFGYTKNLQ NRGRIPNYPA DRTKVFCNTG DLVCTGSLIV 200
    AAPHLAYGPD ARGPAPEFLI EKVRAVRGSA 230
    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 1, 2014
    This is version 109 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