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Reviewed, UniProtKB/Swiss-Prot P85076 (PME_ACTDE)

Last modified October 13, 2009. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pectinesterase
      Short name=PE
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase
OrganismActinidia deliciosa (Kiwi)
Taxonomic identifier3627 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridsEricalesActinidiaceaeActinidia

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Pectin + n H2O = n methanol + pectate. Ref.1

Enzyme regulation

Inhibited by PMEI. Ref.1

Pathway

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

Post-translational modification

The N-glycans attached at Asn-75, Asn-275, Asn-290 and Asn-319 are complex oligosaccharides containing xylose, fucose, hexose and N-acetylglucosamine. Ref.1

Sequence similarities

Belongs to the pectinesterase family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Molecular functionAspartyl esterase
Hydrolase
   PTMAcetylation
Disulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from electronic annotation. Source: InterPro

   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

Chain1 – 321321Pectinesterase
PRO_0000311723

Sites

Active site1371Proton donor By similarity UniProtKB P0C1A8
Active site1581Nucleophile By similarity UniProtKB P0C1A8
Binding site841Substrate By similarity
Binding site1141Substrate By similarity
Binding site2261Substrate By similarity
Binding site2281Substrate By similarity
Site191Not glycosylated
Site1361Transition state stabilizer By similarity

Amino acid modifications

Modified residue11N-acetylthreonine Ref.1
Glycosylation751N-linked (GlcNAc...) (complex) Ref.1
Glycosylation2751N-linked (GlcNAc...) (complex) Ref.1
Glycosylation2901N-linked (GlcNAc...) (complex) Ref.1
Glycosylation3191N-linked (GlcNAc...) (complex) Ref.1
Disulfide bond151 ↔ 171 By similarity

Sequences

Sequence LengthMass (Da)Tools
P85076-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 26CEC95A8071C04D

FASTA32135,368
        10         20         30         40         50         60 
TAVTDIVPDV VVAKDGSGNF TTVGAAVAAA KDSSTARFVI YIKEGAYFEY VDVDKKKTNL 

        70         80         90        100        110        120 
MFIGDGIGKT WIKGNRSVVD GWTTFRSSTV AVVGTGFIAR GISFENYAGP SKHQAVALRS 

       130        140        150        160        170        180 
GADFSAFYQC SFVGYQDTLY VHSLRQFYSE CDVYGTIDFI FGNAAAVLQK CNLYARKPNE 

       190        200        210        220        230        240 
NQKNIFTAQG RDDPNQNTGI SILNCKVAAA ADLIPVLSSF KTYLGRPWKE YSRTVFLLSQ 

       250        260        270        280        290        300 
MESLIDPAGW LEWSGDFALT TLYYREYKNT GPGSNTTARV TWPGYAVTTN ETEVIQFTVG 

       310        320 
NFIQGSQWLT SYNIPVYLNL T 

« Hide

References

[1]"The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor."
Ciardiello M.A., D'Avino R., Amoresano A., Tuppo L., Carpentieri A., Carratore V., Tamburrini M., Giovane A., Pucci P., Camardella L.
Proteins 71:195-206(2007) [PubMed: 17932919] [Abstract]
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ENZYME REGULATION, GLYCOSYLATION AT ASN-75; ASN-275; ASN-290 AND ASN-319, ACETYLATION AT THR-1.
Tissue: Fruit.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.11. 267086.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME_ACTDE
AccessionPrimary (citable) accession number: P85076
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: October 13, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents