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P0C1A8 (PMEA_ERWCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 A
Short name=PE A
EC=3.1.1.11
Alternative name(s):
Pectin methylesterase A
Gene names
Name:pemA
Synonyms:pem
OrganismErwinia chrysanthemi
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in maceration and soft-rotting of plant tissue By similarity.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

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

Subunit structure

Monomer By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the pectinesterase family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcell wall modification

Inferred from electronic annotation. Source: InterPro

pectin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 2424
Chain25 – 366342Pectinesterase A
PRO_0000023498

Sites

Active site1781Proton donor
Active site1991Nucleophile
Binding site1091Substrate By similarity
Binding site1531Substrate By similarity
Binding site2191Substrate By similarity
Binding site2261Substrate By similarity
Binding site2301Substrate By similarity
Binding site2671Substrate By similarity
Binding site2691Substrate By similarity
Binding site2721Substrate; via amide nitrogen and carbonyl oxygen By similarity
Site1771Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond192 ↔ 212

Secondary structure

1 ......................................................................... 366
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C1A8 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: DA7DD9A45290660B

FASTA36639,319
        10         20         30         40         50         60 
MLKTISGTLA LSLIIAASVH QAQAATTYNA VVSKSSSDGK TFKTIADAIA SAPAGSTPFV 

        70         80         90        100        110        120 
ILIKNGVYNE RLTITRNNLL LKGESRNGAV IAAATAAGTL KSDGSKWGTA GSSTITISAK 

       130        140        150        160        170        180 
DFSAQSLTIR NDFDFPANQA KSDSDSSKIK DTQAVALYVT KSGDRAYFKD VSLVGYQDTL 

       190        200        210        220        230        240 
YVSGGRSFFS DCRISGTVDF IFGDGTALFN NCDLVSRYRA DVKSGNVSGY LTAPSTNINQ 

       250        260        270        280        290        300 
KYGLVITNSR VIRESDSVPA KSYGLGRPWH PTTTFSDGRY ADPNAIGQTV FLNTSMDNHI 

       310        320        330        340        350        360 
YGWDKMSGKD KNGNTIWFNP EDSRFFEYKS YGAGAAVSKD RRQLTDAQAA EYTQSKVLGD 


WTPTLP

« Hide

References

[1]"Molecular cloning and nucleotide sequence of the pectin methyl esterase gene of Erwinia chrysanthemi B374."
Plastow G.S.
Mol. Microbiol. 2:247-254(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B374.
[2]"Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site."
Jenkins J., Mayans O., Smith D., Worboys K., Pickersgill R.W.
J. Mol. Biol. 305:951-960(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 25-366.
Strain: B374.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y00549 Genomic DNA. Translation: CAA68628.1.
PIRS03770.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJVX-ray2.37A/B25-366[»]
ProteinModelPortalP0C1A8.
SMRP0C1A8. Positions 25-366.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP0C1A8.
UniPathwayUPA00545; UER00823.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C1A8.

Entry information

Entry namePMEA_ERWCH
AccessionPrimary (citable) accession number: P0C1A8
Secondary accession number(s): P07863
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: April 3, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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