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Q12535 (PME_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pectinesterase

Short name=PE
EC=3.1.1.11
Alternative name(s):
Pectin methylesterase
Gene names
Name:pme1
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in maceration and soft-rotting of plant tissue.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Subcellular location

Secreted.

Sequence similarities

Belongs to the pectinesterase family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

cellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell wall

Inferred from electronic annotation. Source: InterPro

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartyl esterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 331314Pectinesterase
PRO_0000023472

Sites

Active site1621Proton donor By similarity
Active site1831Nucleophile By similarity
Binding site1391Substrate By similarity
Binding site2481Substrate By similarity
Binding site2501Substrate By similarity
Site1611Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12535 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 1F1C81BF1E32174F

FASTA33135,681
        10         20         30         40         50         60 
MVKSVLASAL FAVSALAASR TTAPSGAIVV AKSGGDYTTI GDAIDALSTS TTDTQTIFIE 

        70         80         90        100        110        120 
EGTYDEQVYL PAMTGKVIIY GQTENTDSYA DNLVTITHAI SYEDAGESDD LTATFRNKAV 

       130        140        150        160        170        180 
GSQVYNLNIA NTCGQACHQA LALSAWADQQ GYYGCNFTGY QDTLLAQTGN QLYINSYIEG 

       190        200        210        220        230        240 
AVDFIFGQHA RAWFQNVDIR VVEGPTSASI TANGRSSETD TSYYVINKST VAAKEGDDVA 

       250        260        270        280        290        300 
EGTYYLGRPW SEYARVVFQQ TSMTNVINSL GWTEWSTSTP NTEYVTFGEY ANTGAGSEGT 

       310        320        330 
RASFAEKLDA KLTITDILGS DYTSWVDTSY F 

« Hide

References

[1]"Pectin methyl esterase from Aspergillus aculeatus: expression cloning in yeast and characterization of the recombinant enzyme."
Christgau S., Kofod L.V., Halkier T., Andersen L.N., Hockauf M., Dorreich K., Dalboege H., Kauppinen S.
Biochem. J. 319:705-712(1996) [PubMed: 8920970] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: KSM 510.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49378 mRNA. Translation: AAB42153.1.

3D structure databases

ProteinModelPortalQ12535.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME_ASPAC
AccessionPrimary (citable) accession number: Q12535
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 21, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families