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Protein

Pectinesterase

Gene
N/A
Organism
Daucus carota (Wild carrot)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 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
  2. no protein annotated in this organism
  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 sitei83SubstrateBy similarity1
Binding sitei113SubstrateBy similarity1
Sitei135Transition state stabilizerBy similarity1
Active sitei136Proton donor1
Active sitei157Nucleophile1
Binding sitei225SubstrateBy similarity1
Binding sitei227SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BRENDAi3.1.1.11. 1841.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectinesterase (EC:3.1.1.11)
Short name:
PE
Alternative name(s):
Pectin methylesterase
OrganismiDaucus carota (Wild carrot)
Taxonomic identifieri4039 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucusDaucus sect. Daucus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002150451 – 319PectinesteraseAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1
Disulfide bondi150 ↔ 170By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Beta strandi17 – 21Combined sources5
Helixi22 – 28Combined sources7
Beta strandi37 – 41Combined sources5
Beta strandi43 – 47Combined sources5
Beta strandi50 – 52Combined sources3
Beta strandi58 – 64Combined sources7
Turni66 – 68Combined sources3
Beta strandi69 – 73Combined sources5
Turni77 – 80Combined sources4
Helixi84 – 86Combined sources3
Beta strandi88 – 91Combined sources4
Beta strandi97 – 105Combined sources9
Helixi109 – 111Combined sources3
Beta strandi116 – 119Combined sources4
Beta strandi124 – 132Combined sources9
Beta strandi138 – 140Combined sources3
Beta strandi142 – 149Combined sources8
Beta strandi151 – 157Combined sources7
Beta strandi159 – 162Combined sources4
Beta strandi164 – 169Combined sources6
Beta strandi171 – 174Combined sources4
Beta strandi183 – 188Combined sources6
Beta strandi198 – 203Combined sources6
Beta strandi205 – 208Combined sources4
Turni210 – 212Combined sources3
Helixi213 – 218Combined sources6
Beta strandi221 – 224Combined sources4
Beta strandi232 – 237Combined sources6
Turni254 – 260Combined sources7
Beta strandi262 – 267Combined sources6
Helixi271 – 273Combined sources3
Beta strandi284 – 286Combined sources3
Helixi290 – 294Combined sources5
Helixi298 – 301Combined sources4
Helixi304 – 306Combined sources3
Helixi309 – 311Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQ8X-ray1.75A2-319[»]
ProteinModelPortaliP83218.
SMRiP83218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83218.

Family & Domainsi

Sequence similaritiesi

Belongs to the pectinesterase family.Curated

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
IPR018040. Pectinesterase_Tyr_AS.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QSSTVTPNVV VAADGSGDYK TVSEAVAAAP EDSKTRYVIR IKAGVYRENV
60 70 80 90 100
DVPKKKKNIM FLGDGRTSTI ITASKNVQDG STTFNSATVA AVGAGFLARD
110 120 130 140 150
ITFQNTAGAA KHQAVALRVG SDLSAFYRCD ILAYQDSLYV HSNRQFFINC
160 170 180 190 200
FIAGTVDFIF GNAAVVLQDC DIHARRPGSG QKNMVTAQGR TDPNQNTGIV
210 220 230 240 250
IQKSRIGATS DLQPVQSSFP TYLGRPWKEY SRTVVMQSSI TNVINPAGWF
260 270 280 290 300
PWDGNFALDT LYYGEYQNTG AGAATSGRVT WKGFKVITSS TEAQGFTPGS
310
FIAGGSWLKA TTFPFSLGL
Length:319
Mass (Da):34,254
Last modified:May 2, 2002 - v1
Checksum:i359675FF36FD7625
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQ8X-ray1.75A2-319[»]
ProteinModelPortaliP83218.
SMRiP83218.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BRENDAi3.1.1.11. 1841.

Miscellaneous databases

EvolutionaryTraceiP83218.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
IPR018040. Pectinesterase_Tyr_AS.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPME_DAUCA
AccessioniPrimary (citable) accession number: P83218
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: November 2, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.