Q12535 (PME_ASPAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 54.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pectinesterase Short name=PE EC=3.1.1.11 Alternative name(s): Pectin methylesterase | ||
| Gene names |
| ||
| Organism | Aspergillus aculeatus | ||
| Taxonomic identifier | 5053 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 331 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the pectinesterase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Aspartyl esterase Hydrolase |
| Gene Ontology (GO) | |
| Biological process | cell wall modification Inferred from electronic annotation. Source: InterPro cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell wall Inferred from electronic annotation. Source: InterPro extracellular regionInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW pectinesterase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | By similarity | ||||||
| Chain | 18 – 331 | 314 | Pectinesterase | PRO_0000023472 | |||||
Sites | |||||||||
| Active site | 162 | 1 | Proton donor By similarity | ||||||
| Active site | 183 | 1 | Nucleophile By similarity | ||||||
| Binding site | 139 | 1 | Substrate By similarity | ||||||
| Binding site | 248 | 1 | Substrate By similarity | ||||||
| Binding site | 250 | 1 | Substrate By similarity | ||||||
| Site | 161 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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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 | |
| ProteinModelPortal | Q12535. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. [Graphical view] |
| Gene3D | G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit. |
| Pfam | PF01095. Pectinesterase. 1 hit. [Graphical view] |
| SUPFAM | SSF51126. Pectin_lyas_like. 1 hit. |
| PROSITE | PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PME_ASPAC | ||||||||
| Accession | Primary (citable) accession number: Q12535 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with