Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cutinase 1

Gene

CUT1

Organism
Fusarium solani subsp. pisi (Nectria haematococca)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei1361
Active sitei1911
Active sitei2041

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.74 2361

Protein family/group databases

ESTHERifusso-cutas Cutinase

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176862

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000000644032 – 230Cutinase 1Add BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32N-D-glucuronoyl glycine1 Publication1
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

Proteomic databases

PRIDEiP00590

PTM databases

GlyConnecti116
UniCarbKBiP00590

Expressioni

Inductioni

By contact with cutin.

Structurei

Secondary structure

1230
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni38 – 41Combined sources4
Helixi44 – 46Combined sources3
Beta strandi49 – 55Combined sources7
Turni62 – 67Combined sources6
Helixi68 – 79Combined sources12
Turni81 – 83Combined sources3
Beta strandi84 – 88Combined sources5
Helixi97 – 101Combined sources5
Helixi108 – 124Combined sources17
Beta strandi129 – 135Combined sources7
Helixi138 – 148Combined sources11
Helixi151 – 154Combined sources4
Beta strandi157 – 164Combined sources8
Turni166 – 173Combined sources8
Helixi180 – 182Combined sources3
Beta strandi183 – 186Combined sources4
Helixi192 – 195Combined sources4
Helixi202 – 205Combined sources4
Helixi208 – 212Combined sources5
Helixi214 – 227Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
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
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000675 Cutinase/axe
IPR011150 Cutinase_monf
PfamiView protein in Pfam
PF01083 Cutinase, 1 hit
PRINTSiPR00129 CUTINASE
SMARTiView protein in SMART
SM01110 Cutinase, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00155 CUTINASE_1, 1 hit
PS00931 CUTINASE_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti48R → A in AAA33335 (PubMed:2703464).Curated1
Sequence conflicti94R → A in AAA33335 (PubMed:2703464).Curated1

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiCUTI1_FUSSO
AccessioniPrimary (citable) accession number: P00590
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 124 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health