P17872 (PME_ASPTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 73.
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 tubingensis | ||
| Taxonomic identifier | 5068 [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 protein 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. |
| Caution | Strain RH 5344 was previously said to be from A.niger. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Aspartyl esterase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | cell wall modification Inferred from electronic annotation. Source: InterPro pectin catabolic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| 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 | |||||||
| Chain | 18 – 331 | 314 | Pectinesterase | PRO_0000023473 | |||||
Sites | |||||||||
| Active site | 161 | 1 | Proton donor By similarity | ||||||
| Active site | 182 | 1 | Nucleophile By similarity | ||||||
| Binding site | 138 | 1 | Substrate By similarity | ||||||
| Binding site | 247 | 1 | Substrate By similarity | ||||||
| Binding site | 249 | 1 | Substrate By similarity | ||||||
| Site | 160 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Nucleotide and derived amino acid sequence of a pectinesterase cDNA isolated from Aspergillus niger strain RH 5344." Khanh N.Q., Albrecht H., Ruttkowski E., Loeffler F., Gottschalk M., Jany K.-D. Nucleic Acids Res. 18:4262-4262(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: RH 5344. |
| [2] | "Characterization and expression of a genomic pectin methyl esterase-encoding gene in Aspergillus niger." Khanh N.Q., Ruttkowski E., Leidinger K., Albrecht H., Gottschalk M. Gene 106:71-77(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X52902 mRNA. Translation: CAA37084.1. X54145 Genomic DNA. Translation: CAA38084.1. |
| PIR | JT0589. |
3D structure databases | |
| ProteinModelPortal | P17872. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00545; UER00823. |
Family and domain databases | |
| Gene3D | 2.160.20.10. 1 hit. |
| InterPro | IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. [Graphical view] |
| 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_ASPTU | ||||||||
| Accession | Primary (citable) accession number: P17872 | ||||||||
| Entry history |
| ||||||||
| 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
