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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 (PMEU1), Pectinesterase, 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)DescriptionActionsGraphical viewLength
Binding sitei308SubstrateBy similarity1
Binding sitei338SubstrateBy similarity1
Sitei360Transition state stabilizerBy similarity1
Active sitei361Proton donorPROSITE-ProRule annotation1
Active sitei382NucleophilePROSITE-ProRule annotation1
Binding sitei450SubstrateBy similarity1
Binding sitei452SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
PropeptideiPRO_000002348640 – 2291 PublicationAdd BLAST190
ChainiPRO_0000023487230 – 546Pectinesterase 1Add BLAST317

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi327 ↔ 3541 Publication
Disulfide bondi395 ↔ 4291 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP14280.
PRIDEiP14280.

Expressioni

Developmental stagei

In ripening fruit.

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc07g064170.2.1.

Structurei

Secondary structure

1546
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi233 – 236Combined sources4
Beta strandi242 – 246Combined sources5
Helixi247 – 253Combined sources7
Beta strandi262 – 266Combined sources5
Beta strandi268 – 272Combined sources5
Beta strandi275 – 277Combined sources3
Beta strandi283 – 289Combined sources7
Turni291 – 293Combined sources3
Beta strandi294 – 298Combined sources5
Turni302 – 305Combined sources4
Helixi309 – 311Combined sources3
Beta strandi313 – 316Combined sources4
Beta strandi322 – 325Combined sources4
Beta strandi327 – 330Combined sources4
Helixi334 – 336Combined sources3
Beta strandi341 – 344Combined sources4
Beta strandi349 – 353Combined sources5
Beta strandi355 – 357Combined sources3
Beta strandi363 – 365Combined sources3
Beta strandi367 – 374Combined sources8
Beta strandi376 – 382Combined sources7
Beta strandi384 – 386Combined sources3
Beta strandi389 – 394Combined sources6
Beta strandi396 – 399Combined sources4
Beta strandi408 – 413Combined sources6
Beta strandi423 – 428Combined sources6
Beta strandi430 – 433Combined sources4
Turni435 – 437Combined sources3
Helixi438 – 440Combined sources3
Turni441 – 443Combined sources3
Beta strandi446 – 449Combined sources4
Beta strandi457 – 462Combined sources6
Turni479 – 485Combined sources7
Beta strandi487 – 492Combined sources6
Beta strandi509 – 512Combined sources4
Helixi515 – 518Combined sources4
Helixi519 – 521Combined sources3
Helixi523 – 526Combined sources4
Helixi530 – 533Combined sources4
Helixi534 – 536Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XG2X-ray1.90A230-546[»]
ProteinModelPortaliP14280.
SMRiP14280.
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.
OrthoDBiEOG093608YE.

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)DescriptionActionsGraphical viewLength
Sequence conflicti204F → L in AAB67740 (Ref. 2) Curated1
Sequence conflicti278A → S in AAB67740 (Ref. 2) Curated1
Sequence conflicti430N → D in AAB67740 (Ref. 2) Curated1
Sequence conflicti440V → L in AAB67740 (Ref. 2) Curated1
Sequence conflicti519M → I in AAB67740 (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XG2X-ray1.90A230-546[»]
ProteinModelPortaliP14280.
SMRiP14280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc07g064170.2.1.

Proteomic databases

PaxDbiP14280.
PRIDEiP14280.

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.
OrthoDBiEOG093608YE.

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...

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: November 30, 2016
This is version 135 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.