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Reviewed, UniProtKB/Swiss-Prot P14280 (PME1_SOLLC)

Last modified February 9, 2010. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Pectinesterase 1
      Short name=PE 1
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 1
Gene names
Name: PME1.9
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

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Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening.

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

Secreted › cell wall.

Developmental stage

In ripening fruit.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Propeptide40 – 229190
PRO_0000023486
Chain230 – 546317Pectinesterase 1
PRO_0000023487

Sites

Active site3611Proton donor By similarity
Active site3821Nucleophile By similarity
Binding site3081Substrate By similarity
Binding site3381Substrate By similarity
Binding site4501Substrate By similarity
Binding site4521Substrate By similarity
Site3601Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond327 ↔ 354 Ref.6
Disulfide bond395 ↔ 429 Ref.6

Experimental info

Sequence conflict2041F → L in AAB67740. Ref.2
Sequence conflict2781A → S in AAB67740. Ref.2
Sequence conflict4301N → D in AAB67740. Ref.2
Sequence conflict4401V → L in AAB67740. Ref.2
Sequence conflict5191M → I in AAB67740. Ref.2

Secondary structure

1 ........................................................................... 546
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14280-1 [UniParc].

Last modified July 15, 1999. Version 5.
Checksum: 4FEDF511FF075DCB

FASTA54660,066
        10         20         30         40         50         60 
MANPQQPLLI KTHKQNPIIS FKILSFVITL FVALFLVAPY QVEIKHSNLC KTAQDSQLCL 

        70         80         90        100        110        120 
SYVSDLISNE IVTTESDGHS ILMKFLVNYV HQMNNAIPVV RKMKNQINDI RQHGALTDCL 

       130        140        150        160        170        180 
ELLDQSVDFA SDSIAAIDKR SRSEHANAQS WLSGVLTNHV TCLDELDSFT KAMINGTNLE 

       190        200        210        220        230        240 
ELISRAKVAL AMLASLTTQD EDVFMTVLGK MPSWVSSMDR KLMESSGKDI IANAVVAQDG 

       250        260        270        280        290        300 
TGDYQTLAEA VAAAPDKSKT RYVIYVKRGT YKENVEVASN KMNLMIVGDG MYATTITGSL 

       310        320        330        340        350        360 
NVVDGSTTFR SATLAAVGQG FILQDICIQN TAGPAKDQAV ALRVGADMSV INRCRIDAYQ 

       370        380        390        400        410        420 
DTLYAHSQRQ FYRDSYVTGT VDFIFGNAAV VFQKCQLVAR KPGKYQQNMV TAQGRTDPNQ 

       430        440        450        460        470        480 
ATGTSIQFCN IIASSDLEPV LKEFPTYLGR PWKEYSRTVV MESYLGGLIN PAGWAEWDGD 

       490        500        510        520        530        540 
FALKTLYYGE FMNNGPGAGT SKRVKWPGYH VITDPAKAMP FTVAKLIQGG SWLRSTGVAY 


VDGLYD

« Hide

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References

[1]"Molecular characterisation of cDNA clones representing pectin esterase isozymes from tomato."
Hall L.N., Bird C.R., Picton S., Tucker G.A., Seymour G.B., Grierson D.
Plant Mol. Biol. 25:313-318(1994) [PubMed: 8018878] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Ailsa Craig.
Tissue: Pericarp.
[2]"Isolation and nucleotide sequence of two cDNAs corresponding to tomato fruit pectin methylesterase genes."
Turner L.A., Kausch K.D., Handa A.K.
Plant Gene Register PGR96-035
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-546.
Strain: cv. Rutgers.
[3]"Pectinesterase. The primary structure of the tomato enzyme."
Markovic O., Joernvall H.
Eur. J. Biochem. 158:455-462(1986) [PubMed: 3732279] [Abstract]
Cited for: PROTEIN SEQUENCE OF 230-546.
[4]"Tomato and Aspergillus niger pectinesterases. Correlation of differences in existing reports: large species variations."
Markovic O., Joernvall H.
Protein Seq. Data Anal. 3:513-515(1990) [PubMed: 2089377] [Abstract]
Cited for: SEQUENCE REVISION.
[5]Markovic O., Joernvall H.
Submitted (MAR-1996) to UniProtKB
Cited for: SEQUENCE REVISION.
[6]"Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments."
Markovic O., Joernvall H.
Protein Sci. 1:1288-1292(1992) [PubMed: 1303747] [Abstract]
Cited for: DISULFIDE BONDS.
[7]"Tomato pectin methylesterase: modeling, fluorescence, and inhibitor interaction studies-comparison with the bacterial (Erwinia chrysanthemi) enzyme."
D'Avino R., Camardella L., Christensen T.M., Giovane A., Servillo L.
Proteins 53:830-839(2003) [PubMed: 14635125] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 230-546 IN COMPLEX WITH KIWI PMEI.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X74638 mRNA. Translation: CAA52703.1.
U50986 mRNA. Translation: AAB67740.1.
PIRA25010.
S46527.
UniGeneLes.3122

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XG2X-ray1.90A230-546[»]
SMRP14280. Positions 47-187.
ModBaseSearch...

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME1_SOLLC
AccessionPrimary (citable) accession number: P14280
Secondary accession number(s): Q43145
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 15, 1999
Last modified: February 9, 2010
This is version 100 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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

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