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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)DescriptionActionsGraphical viewLength
Active sitei1361
Active sitei1911
Active sitei2041

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, 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

GO - Cellular componenti

Complete GO annotation...

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

PTM databases

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
Helixi137 – 148Combined sources12
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.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase/axe.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
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)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.

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
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...

Chemistry databases

ChEMBLiCHEMBL2176862.

Protein family/group databases

ESTHERifusso-cutas. Cutinase.

PTM databases

UniCarbKBiP00590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.74. 2361.

Miscellaneous databases

EvolutionaryTraceiP00590.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000675. Cutinase/axe.
IPR011150. Cutinase_monf.
[Graphical view]
PfamiPF01083. Cutinase. 1 hit.
[Graphical view]
PRINTSiPR00129. CUTINASE.
SMARTiSM01110. Cutinase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 120 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

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 one 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.