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P83218 (PME_DAUCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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

Short name=PE
EC=3.1.1.11
Alternative name(s):
Pectin methylesterase
OrganismDaucus carota (Carrot)
Taxonomic identifier4039 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucus

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the deesterification of methyl-esterified D-galactosiduronic acid units in pectic compounds. It participates in modulating cell wall during fruit ripening, cell wall extension during pollen germination, and in defense mechanisms against pathogens.

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

Secretedcell wall Probable.

Sequence similarities

Belongs to the pectinesterase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Pectinesterase
PRO_0000215045

Sites

Active site1361Proton donor
Active site1571Nucleophile
Binding site831Substrate By similarity
Binding site1131Substrate By similarity
Binding site2251Substrate By similarity
Binding site2271Substrate By similarity
Site1351Transition state stabilizer By similarity

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Disulfide bond150 ↔ 170 By similarity

Secondary structure

........................................................................ 319
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P83218 [UniParc].

Last modified May 2, 2002. Version 1.
Checksum: 359675FF36FD7625

FASTA31934,254
        10         20         30         40         50         60 
QSSTVTPNVV VAADGSGDYK TVSEAVAAAP EDSKTRYVIR IKAGVYRENV DVPKKKKNIM 

        70         80         90        100        110        120 
FLGDGRTSTI ITASKNVQDG STTFNSATVA AVGAGFLARD ITFQNTAGAA KHQAVALRVG 

       130        140        150        160        170        180 
SDLSAFYRCD ILAYQDSLYV HSNRQFFINC FIAGTVDFIF GNAAVVLQDC DIHARRPGSG 

       190        200        210        220        230        240 
QKNMVTAQGR TDPNQNTGIV IQKSRIGATS DLQPVQSSFP TYLGRPWKEY SRTVVMQSSI 

       250        260        270        280        290        300 
TNVINPAGWF PWDGNFALDT LYYGEYQNTG AGAATSGRVT WKGFKVITSS TEAQGFTPGS 

       310 
FIAGGSWLKA TTFPFSLGL 

« Hide

References

[1]"Characterization of carrot pectin methylesterase."
Markovic O., Cederlund E., Griffiths W.J., Lipka T., Joernvall H.
Cell. Mol. Life Sci. 59:513-518(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: cv. Tiptop.
Tissue: Root.
[2]"Crystal structure of plant pectin methylesterase."
Johansson K., El-Ahmad M., Friemann R., Joernvall H., Markovic O., Eklund H.
FEBS Lett. 514:243-249(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), CHARACTERIZATION.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQ8X-ray1.75A2-319[»]
ProteinModelPortalP83218.
SMRP83218. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.11. 1841.
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. SSF51126. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP83218.

Entry information

Entry namePME_DAUCA
AccessionPrimary (citable) accession number: P83218
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: February 19, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways