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P83218

- PME_DAUCA

UniProt

P83218 - PME_DAUCA

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Protein

Pectinesterase

Gene
N/A
Organism
Daucus carota (Wild carrot)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831SubstrateBy similarity
Binding sitei113 – 1131SubstrateBy similarity
Sitei135 – 1351Transition state stabilizerBy similarity
Active sitei136 – 1361Proton donor
Active sitei157 – 1571Nucleophile
Binding sitei225 – 2251SubstrateBy similarity
Binding sitei227 – 2271SubstrateBy similarity

GO - Molecular functioni

  1. aspartyl esterase activity Source: UniProtKB-KW
  2. pectinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall modification Source: InterPro
  2. pectin catabolic process Source: UniProtKB-UniPathway
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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucus

Subcellular locationi

Secretedcell wall Curated

GO - Cellular componenti

  1. cell wall Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319PectinesterasePRO_0000215045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi150 ↔ 170By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Beta strandi17 – 215Combined sources
Helixi22 – 287Combined sources
Beta strandi37 – 415Combined sources
Beta strandi43 – 475Combined sources
Beta strandi50 – 523Combined sources
Beta strandi58 – 647Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 735Combined sources
Turni77 – 804Combined sources
Helixi84 – 863Combined sources
Beta strandi88 – 914Combined sources
Beta strandi97 – 1059Combined sources
Helixi109 – 1113Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi124 – 1329Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi142 – 1498Combined sources
Beta strandi151 – 1577Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi205 – 2084Combined sources
Turni210 – 2123Combined sources
Helixi213 – 2186Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi232 – 2376Combined sources
Turni254 – 2607Combined sources
Beta strandi262 – 2676Combined sources
Helixi271 – 2733Combined sources
Beta strandi284 – 2863Combined sources
Helixi290 – 2945Combined sources
Helixi298 – 3014Combined sources
Helixi304 – 3063Combined sources
Helixi309 – 3113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQ8X-ray1.75A2-319[»]
ProteinModelPortaliP83218.
SMRiP83218. Positions 1-319.
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.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[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
Entry Method Resolution (Å) Chain Positions PDBsum
1GQ8 X-ray 1.75 A 2-319 [» ]
ProteinModelPortali P83218.
SMRi P83218. Positions 1-319.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00545 ; UER00823 .
BRENDAi 3.1.1.11. 1841.

Miscellaneous databases

EvolutionaryTracei P83218.

Family and domain databases

Gene3Di 2.160.20.10. 1 hit.
InterProi IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view ]
Pfami PF01095. Pectinesterase. 1 hit.
[Graphical view ]
SUPFAMi SSF51126. SSF51126. 1 hit.
PROSITEi PS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: PROTEIN SEQUENCE.
    Strain: cv. Tiptop.
    Tissue: Root.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), CHARACTERIZATION.

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 26, 2014
This is version 70 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

External Data

Dasty 3