Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P83218

- PME_DAUCA

UniProt

P83218 - PME_DAUCA

Protein

Pectinesterase

Gene
N/A
Organism
Daucus carota (Wild carrot)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (02 May 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell
    2. extracellular region Source: UniProtKB-KW

    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 – 114
    Beta strandi17 – 215
    Helixi22 – 287
    Beta strandi37 – 415
    Beta strandi43 – 475
    Beta strandi50 – 523
    Beta strandi58 – 647
    Turni66 – 683
    Beta strandi69 – 735
    Turni77 – 804
    Helixi84 – 863
    Beta strandi88 – 914
    Beta strandi97 – 1059
    Helixi109 – 1113
    Beta strandi116 – 1194
    Beta strandi124 – 1329
    Beta strandi138 – 1403
    Beta strandi142 – 1498
    Beta strandi151 – 1577
    Beta strandi159 – 1624
    Beta strandi164 – 1696
    Beta strandi171 – 1744
    Beta strandi183 – 1886
    Beta strandi198 – 2036
    Beta strandi205 – 2084
    Turni210 – 2123
    Helixi213 – 2186
    Beta strandi221 – 2244
    Beta strandi232 – 2376
    Turni254 – 2607
    Beta strandi262 – 2676
    Helixi271 – 2733
    Beta strandi284 – 2863
    Helixi290 – 2945
    Helixi298 – 3014
    Helixi304 – 3063
    Helixi309 – 3113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    QSSTVTPNVV VAADGSGDYK TVSEAVAAAP EDSKTRYVIR IKAGVYRENV    50
    DVPKKKKNIM FLGDGRTSTI ITASKNVQDG STTFNSATVA AVGAGFLARD 100
    ITFQNTAGAA KHQAVALRVG SDLSAFYRCD ILAYQDSLYV HSNRQFFINC 150
    FIAGTVDFIF GNAAVVLQDC DIHARRPGSG QKNMVTAQGR TDPNQNTGIV 200
    IQKSRIGATS DLQPVQSSFP TYLGRPWKEY SRTVVMQSSI TNVINPAGWF 250
    PWDGNFALDT LYYGEYQNTG AGAATSGRVT WKGFKVITSS TEAQGFTPGS 300
    FIAGGSWLKA TTFPFSLGL 319
    Length:319
    Mass (Da):34,254
    Last modified:May 2, 2002 - v1
    Checksum:i359675FF36FD7625
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 68 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