Reviewed,
UniProtKB/Swiss-Prot Q47474 (PMEB_DICD3)
Last modified
January 19, 2010.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pectinesterase B Short name=PE B EC=3.1.1.11 Alternative name(s): Pectin methylesterase B | ||
| Gene names |
| ||
| Organism | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) | ||
| Taxonomic identifier | 198628 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya |
Protein attributes
| Sequence length | 433 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 | Probably involved in the degradation of methylated oligogalacturonides present in the periplasm. |
| 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 | |
| Induction | By pectin. |
| Sequence similarities | Belongs to the pectinesterase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Cell outer membrane Membrane |
| Domain | Signal |
| Molecular function | Aspartyl esterase Hydrolase |
| PTM | Lipoprotein Palmitate |
| Gene Ontology (GO) | |
| Biological process | cell wall modification Inferred from electronic annotation. Source: InterPro |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell outer membraneInferred from electronic annotation. Source: UniProtKB-KW cell wallInferred from electronic annotation. Source: InterPro plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 21 | 21 | |||||||
| Chain | 22 – 433 | 412 | Pectinesterase B | PRO_0000023499 | |||||
Sites | |||||||||
| Active site | 259 | 1 | Proton donor By similarity | ||||||
| Active site | 292 | 1 | Nucleophile By similarity | ||||||
| Binding site | 202 | 1 | Substrate By similarity | ||||||
| Binding site | 236 | 1 | Substrate By similarity | ||||||
| Binding site | 356 | 1 | Substrate By similarity | ||||||
| Binding site | 358 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Lipidation | 22 | 1 | N-palmitoyl cysteine | ||||||
| Lipidation | 22 | 1 | S-diacylglycerol cysteine Probable | ||||||
Sequences
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References
| [1] | "Characterization of pectin methylesterase B, an outer membrane lipoprotein of Erwinia chrysanthemi 3937." Shevchik V.E., Condemine G., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J. Mol. Microbiol. 19:455-466(1996) [PubMed: 8830237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PALMITOYLATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X84665 Genomic DNA. Translation: CAA59151.1. |
| PIR | S70914. |
3D structure databases | |
| SMR | Q47474. Positions 83-396. |
| ModBase | 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] |
| PROSITE | PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PMEB_DICD3 | ||||||||
| Accession | Primary (citable) accession number: Q47474 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


