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Protein

Pectinesterase 1

Gene

PME1.9

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Pectin + n H2O = n methanol + pectate.

Pathwayi: pectin degradation

This protein is involved in step 1 of the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase 1 (PME1.9), Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase 2.1 (PME2.1), Pectinesterase, Pectinesterase, Pectinesterase (PMEU1), Pectinesterase, Pectinesterase, Pectinesterase 2.2 (PME2.2), Pectinesterase, Pectinesterase (LePME1), Pectinesterase 3 (PME3), Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase/pectinesterase inhibitor U1 (PMEU1), Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase, Pectinesterase
  2. Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Probable pectate lyase P59 (LAT59), Probable pectate lyase P56 (LAT56), Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Pectate lyase, Probable pectate lyase P18 (9612), Pectate lyase, Pectate lyase
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway pectin degradation, which is itself part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin, the pathway pectin degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei308 – 3081SubstrateBy similarity
Binding sitei338 – 3381SubstrateBy similarity
Sitei360 – 3601Transition state stabilizerBy similarity
Active sitei361 – 3611Proton donorPROSITE-ProRule annotation
Active sitei382 – 3821NucleophilePROSITE-ProRule annotation
Binding sitei450 – 4501SubstrateBy similarity
Binding sitei452 – 4521SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Fruit ripening

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16134.
BRENDAi3.1.1.11. 3101.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectinesterase 1 (EC:3.1.1.11)
Short name:
PE 1
Alternative name(s):
Pectin methylesterase 1
Gene namesi
Name:PME1.9
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
Proteomesi
  • UP000004994 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence analysisAdd
BLAST
Propeptidei40 – 2291901 PublicationPRO_0000023486Add
BLAST
Chaini230 – 546317Pectinesterase 1PRO_0000023487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi327 ↔ 3541 Publication
Disulfide bondi395 ↔ 4291 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP14280.

Expressioni

Developmental stagei

In ripening fruit.

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc07g064170.2.1.

Structurei

Secondary structure

1
546
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi233 – 2364Combined sources
Beta strandi242 – 2465Combined sources
Helixi247 – 2537Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi268 – 2725Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi283 – 2897Combined sources
Turni291 – 2933Combined sources
Beta strandi294 – 2985Combined sources
Turni302 – 3054Combined sources
Helixi309 – 3113Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi327 – 3304Combined sources
Helixi334 – 3363Combined sources
Beta strandi341 – 3444Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi367 – 3748Combined sources
Beta strandi376 – 3827Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi389 – 3946Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi408 – 4136Combined sources
Beta strandi423 – 4286Combined sources
Beta strandi430 – 4334Combined sources
Turni435 – 4373Combined sources
Helixi438 – 4403Combined sources
Turni441 – 4433Combined sources
Beta strandi446 – 4494Combined sources
Beta strandi457 – 4626Combined sources
Turni479 – 4857Combined sources
Beta strandi487 – 4926Combined sources
Beta strandi509 – 5124Combined sources
Helixi515 – 5184Combined sources
Helixi519 – 5213Combined sources
Helixi523 – 5264Combined sources
Helixi530 – 5334Combined sources
Helixi534 – 5363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XG2X-ray1.90A230-546[»]
ProteinModelPortaliP14280.
SMRiP14280. Positions 230-546.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14280.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II3N. Eukaryota.
COG4677. LUCA.
InParanoidiP14280.
KOiK01051.
OMAiNKMNLMI.

Family and domain databases

Gene3Di1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib_dom.
IPR018040. Pectinesterase_Tyr_AS.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTiSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMiSSF101148. SSF101148. 1 hit.
SSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR01614. PME_inhib. 1 hit.
PROSITEiPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANPQQPLLI KTHKQNPIIS FKILSFVITL FVALFLVAPY QVEIKHSNLC
60 70 80 90 100
KTAQDSQLCL SYVSDLISNE IVTTESDGHS ILMKFLVNYV HQMNNAIPVV
110 120 130 140 150
RKMKNQINDI RQHGALTDCL ELLDQSVDFA SDSIAAIDKR SRSEHANAQS
160 170 180 190 200
WLSGVLTNHV TCLDELDSFT KAMINGTNLE ELISRAKVAL AMLASLTTQD
210 220 230 240 250
EDVFMTVLGK MPSWVSSMDR KLMESSGKDI IANAVVAQDG TGDYQTLAEA
260 270 280 290 300
VAAAPDKSKT RYVIYVKRGT YKENVEVASN KMNLMIVGDG MYATTITGSL
310 320 330 340 350
NVVDGSTTFR SATLAAVGQG FILQDICIQN TAGPAKDQAV ALRVGADMSV
360 370 380 390 400
INRCRIDAYQ DTLYAHSQRQ FYRDSYVTGT VDFIFGNAAV VFQKCQLVAR
410 420 430 440 450
KPGKYQQNMV TAQGRTDPNQ ATGTSIQFCN IIASSDLEPV LKEFPTYLGR
460 470 480 490 500
PWKEYSRTVV MESYLGGLIN PAGWAEWDGD FALKTLYYGE FMNNGPGAGT
510 520 530 540
SKRVKWPGYH VITDPAKAMP FTVAKLIQGG SWLRSTGVAY VDGLYD
Length:546
Mass (Da):60,066
Last modified:July 15, 1999 - v5
Checksum:i4FEDF511FF075DCB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041F → L in AAB67740 (Ref. 2) Curated
Sequence conflicti278 – 2781A → S in AAB67740 (Ref. 2) Curated
Sequence conflicti430 – 4301N → D in AAB67740 (Ref. 2) Curated
Sequence conflicti440 – 4401V → L in AAB67740 (Ref. 2) Curated
Sequence conflicti519 – 5191M → I in AAB67740 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74638 mRNA. Translation: CAA52703.1.
U50986 mRNA. Translation: AAB67740.1.
PIRiA25010.
S46527.
RefSeqiNP_001234151.1. NM_001247222.2.
UniGeneiLes.21898.
Les.3122.

Genome annotation databases

EnsemblPlantsiSolyc07g064170.2.1; Solyc07g064170.2.1; Solyc07g064170.2.
GeneIDi544090.
GrameneiSolyc07g064170.2.1; Solyc07g064170.2.1; Solyc07g064170.2.
KEGGisly:544090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74638 mRNA. Translation: CAA52703.1.
U50986 mRNA. Translation: AAB67740.1.
PIRiA25010.
S46527.
RefSeqiNP_001234151.1. NM_001247222.2.
UniGeneiLes.21898.
Les.3122.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XG2X-ray1.90A230-546[»]
ProteinModelPortaliP14280.
SMRiP14280. Positions 230-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc07g064170.2.1.

Proteomic databases

PaxDbiP14280.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiSolyc07g064170.2.1; Solyc07g064170.2.1; Solyc07g064170.2.
GeneIDi544090.
GrameneiSolyc07g064170.2.1; Solyc07g064170.2.1; Solyc07g064170.2.
KEGGisly:544090.

Phylogenomic databases

eggNOGiENOG410II3N. Eukaryota.
COG4677. LUCA.
InParanoidiP14280.
KOiK01051.
OMAiNKMNLMI.

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BioCyciMetaCyc:MONOMER-16134.
BRENDAi3.1.1.11. 3101.

Miscellaneous databases

EvolutionaryTraceiP14280.

Family and domain databases

Gene3Di1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib_dom.
IPR018040. Pectinesterase_Tyr_AS.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTiSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMiSSF101148. SSF101148. 1 hit.
SSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR01614. PME_inhib. 1 hit.
PROSITEiPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 230-546 IN COMPLEX WITH KIWI PMEI.

Entry informationi

Entry nameiPME1_SOLLC
AccessioniPrimary (citable) accession number: P14280
Secondary accession number(s): Q43145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 15, 1999
Last modified: July 6, 2016
This is version 131 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.