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Protein

Cutinase 1

Gene

cutL

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Seems, in this nonpathogenic fungi, to play an important role in flavor formation.

Catalytic activityi

Cutin + H2O = cutin monomers.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei126By similarity1
Active sitei181By similarity1
Active sitei194By similarity1

GO - Molecular functioni

  • cutinase activity Source: ASPGD

GO - Biological processi

  • lipid catabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERiaspor-cutas. Cutinase.

Names & Taxonomyi

Protein namesi
Recommended name:
Cutinase 1 (EC:3.1.1.74)
Alternative name(s):
Cutin hydrolase 1
Short name:
L1
Gene namesi
Name:cutL
ORF Names:AO090005000029
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000000643417 – 213Cutinase 1Add BLAST197

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi37 ↔ 184By similarity
Disulfide bondi115 ↔ 177By similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 30Combined sources3
Helixi31 – 34Combined sources4
Beta strandi39 – 45Combined sources7
Turni52 – 54Combined sources3
Helixi58 – 69Combined sources12
Turni70 – 72Combined sources3
Beta strandi74 – 78Combined sources5
Helixi87 – 91Combined sources5
Helixi98 – 114Combined sources17
Beta strandi119 – 125Combined sources7
Helixi127 – 136Combined sources10
Helixi141 – 146Combined sources6
Beta strandi147 – 154Combined sources8
Turni156 – 163Combined sources8
Helixi170 – 172Combined sources3
Beta strandi173 – 176Combined sources4
Helixi182 – 185Combined sources4
Helixi192 – 195Combined sources4
Helixi197 – 200Combined sources4
Helixi201 – 211Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GBSX-ray1.75A17-213[»]
3QPDX-ray1.57A26-212[»]
ProteinModelPortaliP52956.
SMRiP52956.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52956.

Family & Domainsi

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171425.
OMAiCKDITFI.
OrthoDBiEOG092C4OIR.

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.

P52956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLRNIVIAL AATAVASPVD LQDRQLTGGD ELRDGPCKPI TFIFARASTE
60 70 80 90 100
PGLLGISTGP AVCNRLKLAR SGDVACQGVG PRYTADLPSN ALPEGTSQAA
110 120 130 140 150
IAEAQGLFEQ AVSKCPDTQI VAGGYSQGTA VMNGAIKRLS ADVQDKIKGV
160 170 180 190 200
VLFGYTRNAQ ERGQIANFPK DKVKVYCAVG DLVCLGTLIV APPHFSYLSD
210
TGDASDFLLS QLG
Length:213
Mass (Da):22,263
Last modified:October 1, 1996 - v1
Checksum:i2213317B4A14A0CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38311 Genomic DNA. Translation: BAA07428.1.
AP007151 Genomic DNA. Translation: BAE55151.1.
RefSeqiXP_001817153.1. XM_001817101.2.

Genome annotation databases

EnsemblFungiiBAE55151; BAE55151; AO090005000029.
GeneIDi5989098.
KEGGiaor:AOR_1_52174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38311 Genomic DNA. Translation: BAA07428.1.
AP007151 Genomic DNA. Translation: BAE55151.1.
RefSeqiXP_001817153.1. XM_001817101.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GBSX-ray1.75A17-213[»]
3QPDX-ray1.57A26-212[»]
ProteinModelPortaliP52956.
SMRiP52956.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspor-cutas. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE55151; BAE55151; AO090005000029.
GeneIDi5989098.
KEGGiaor:AOR_1_52174.

Phylogenomic databases

HOGENOMiHOG000171425.
OMAiCKDITFI.
OrthoDBiEOG092C4OIR.

Miscellaneous databases

EvolutionaryTraceiP52956.

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_ASPOR
AccessioniPrimary (citable) accession number: P52956
Secondary accession number(s): Q2UTG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 93 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, Complete proteome, Reference proteome

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.