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O04887 (PME2_CITSI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pectinesterase 2

Short name=PE 2
EC=3.1.1.11
Alternative name(s):
Pectin methylesterase
Gene names
Name:PECS-2.1
OrganismCitrus sinensis (Sweet orange) (Citrus aurantium var. sinensis)
Taxonomic identifier2711 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsSapindalesRutaceaeCitrus

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts in the modification of cell walls via demethylesterification of cell wall pectin 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.

Subcellular location

Secretedcell wall Probable.

Tissue specificity

Expressed at low levels in young leaves, young bark, young fruit, mature fruit vesicles, shoots and flower buds, young bark and juice vesicles. In both leaf and fruit abscission zones, and mature leaves, expression was initially undetectable but increased markedly following ethylene treatment. Ref.1

Induction

By ethylene. Ref.1

Miscellaneous

The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport.

Sequence similarities

In the N-terminal section; belongs to the PMEI family.

In the C-terminal section; belongs to the pectinesterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 510491Pectinesterase 2
PRO_0000023481

Sites

Active site3281Proton donor By similarity
Active site3491Nucleophile By similarity
Binding site2751Substrate By similarity
Binding site3051Substrate By similarity
Binding site4161Substrate By similarity
Binding site4181Substrate By similarity
Site3271Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation3851N-linked (GlcNAc...) Potential
Disulfide bond342 ↔ 362 By similarity

Experimental info

Sequence conflict1301T → S in AAB57671. Ref.1
Sequence conflict1661T → A in AAB57671. Ref.1
Sequence conflict3871S → N in AAB57671. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O04887 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: BD4D57D0376A2035

FASTA51056,328
        10         20         30         40         50         60 
MALRILITVS LVLFSLSHTS FGYSPEEVKS WCGKTPNPQP CEYFLTQKTD VTSIKQDTDF 

        70         80         90        100        110        120 
YKISLQLALE RATTAQSRTY TLGSKCRNER EKAAWEDCRE LYELTVLKLN QTSNSSPGCT 

       130        140        150        160        170        180 
KVDKQTWLST ALTNLETCRA SLEDLGVPEY VLPLLSNNVT KLISNTLSLN KVPYNEPSYK 

       190        200        210        220        230        240 
DGFPTWVKPG DRKLLQTTPR ANIVVAQDGS GNVKTIQEAV AAASRAGGSR YVIYIKAGTY 

       250        260        270        280        290        300 
NENIEVKLKN IMFVGDGIGK TIITGSKSVG GGATTFKSAT VAVVGDNFIA RDITIRNTAG 

       310        320        330        340        350        360 
PNNHQAVALR SGSDLSVFYR CSFEGYQDTL YVHSQRQFYR ECDIYGTVDF IFGNAAVVLQ 

       370        380        390        400        410        420 
NCNIFARKPP NRTNTLTAQG RTDPNQSTGI IIHNCRVTAA SDLKPVQSSV KTFLGRPWKQ 

       430        440        450        460        470        480 
YSRTVYIKTF LDSLINPAGW MEWSGDFALN TLYYAEYMNT GPGSSTANRV KWRGYHVLTS 

       490        500        510 
PSQVSQFTVG NFIAGNSWLP ATNVPFTSGL 

« Hide

References

[1]"Genetics and expression of two pectinesterase genes in Valencia orange."
Nairn C.J., Lewandowski D.J., Burns J.K.
Physiol. Plantarum 102:226-235(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Valencia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82975 Genomic DNA. Translation: AAB57669.1.
U82977 mRNA. Translation: AAB57671.1.
PIRT10491.
T10494.

3D structure databases

ProteinModelPortalO04887.
SMRO04887. Positions 197-510.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00545; UER00823.

Family and domain databases

Gene3D1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME2_CITSI
AccessionPrimary (citable) accession number: O04887
Secondary accession number(s): O04889
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: March 6, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families