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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261By similarity
Active sitei181 – 1811By similarity
Active sitei194 – 1941By similarity

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

Organism-specific databases

EuPathDBiFungiDB:AO090005000029.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 213197Cutinase 1PRO_0000006434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 184By similarity
Disulfide bondi115 ↔ 177By similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Helixi31 – 344Combined sources
Beta strandi39 – 457Combined sources
Turni52 – 543Combined sources
Helixi58 – 6912Combined sources
Turni70 – 723Combined sources
Beta strandi74 – 785Combined sources
Helixi87 – 915Combined sources
Helixi98 – 11417Combined sources
Beta strandi119 – 1257Combined sources
Helixi127 – 13610Combined sources
Helixi141 – 1466Combined sources
Beta strandi147 – 1548Combined sources
Turni156 – 1638Combined sources
Helixi170 – 1723Combined sources
Beta strandi173 – 1764Combined sources
Helixi182 – 1854Combined sources
Helixi192 – 1954Combined sources
Helixi197 – 2004Combined sources
Helixi201 – 21111Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP52956.

Family & Domainsi

Sequence similaritiesi

Belongs to the cutinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000171425.
OMAiCKDITFI.
OrthoDBiEOG779P8P.

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

EnsemblFungiiCADAORAT00002080; CADAORAP00002049; CADAORAG00002080.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3GBSX-ray1.75A17-213[»]
3QPDX-ray1.57A26-212[»]
ProteinModelPortaliP52956.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiaspor-cutas. Cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00002080; CADAORAP00002049; CADAORAG00002080.
GeneIDi5989098.
KEGGiaor:AOR_1_52174.

Organism-specific databases

EuPathDBiFungiDB:AO090005000029.

Phylogenomic databases

HOGENOMiHOG000171425.
OMAiCKDITFI.
OrthoDBiEOG779P8P.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome structure and nucleotide sequence of a lipolytic enzyme gene of Aspergillus oryzae."
    Ohnishi K., Toida J., Nakazawa H., Sekiguchi J.
    FEMS Microbiol. Lett. 126:145-150(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NBRC 4202.
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

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: May 11, 2016
This is version 90 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.