Q47474 (PMEB_DICD3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
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 B Short name=PE B EC=3.1.1.11 Alternative name(s): Pectin methylesterase B | ||||
| Gene names |
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| Organism | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) [Complete proteome] [HAMAP] | ||||
| 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 |
| Technical term | Complete proteome |
| 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 outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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 Ref.1 | ||||||
| Lipidation | 22 | 1 | S-diacylglycerol cysteine Probable | ||||||
Experimental info | |||||||||
| Sequence conflict | 245 – 258 | 14 | DRVQL…LLSRQ → ESGATGKCPPAQPS in CAA59151. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PALMITOYLATION. Strain: 3937. |
| [2] | "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937." Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N., Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D., Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K., Rauscher L., Rodriguez-Palenzuela P., Toussaint A. Perna N.T.J. Bacteriol. 193:2076-2077(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 3937. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X84665 Genomic DNA. Translation: CAA59151.1. CP002038 Genomic DNA. Translation: ADM98093.1. |
| PIR | S70914. |
| RefSeq | YP_003882650.1. NC_014500.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADM98093; ADM98093; Dda3937_03435. |
| GeneID | 9733317. |
| KEGG | ddd:Dda3937_03435. |
| PATRIC | 42316098. VBIDicDad25310_1873. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000118057. |
| KO | K01051. |
| OMA | FNRMWEY. |
Enzyme and pathway databases | |
| BioCyc | DDAD198628:GHFQ-1931-MONOMER. |
| 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 | PMEB_DICD3 | ||||||||
| Accession | Primary (citable) accession number: Q47474 Secondary accession number(s): E0SL58 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
