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Q3E989 (PME54_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pectinesterase/pectinesterase inhibitor 54

Including the following 2 domains:

  1. Pectinesterase inhibitor 54
    Alternative name(s):
    Pectin methylesterase inhibitor 54
  2. Pectinesterase 54
    Short name=PE 54
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 54
    Short name=AtPME54
Gene names
Name:PME54
Synonyms:ARATH54
Ordered Locus Names:At5g20860
ORF Names:F22D1.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Subcellular location

Secreted › cell wall By similarity.

Tissue specificity

Expressed in siliques. Ref.4

Developmental stage

Expressed during late developmental phases of siliques. Ref.4

Miscellaneous

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

Sequence similarities

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 512488Probable pectinesterase/pectinesterase inhibitor 54
PRO_0000371702

Regions

Region29 – 193165Pectinesterase inhibitor 54
Region229 – 496268Pectinesterase 54

Sites

Active site3251Proton donor; for pectinesterase activity By similarity
Active site3461Nucleophile; for pectinesterase activity By similarity
Binding site3021Substrate; for pectinesterase activity By similarity
Binding site4151Substrate; for pectinesterase activity By similarity
Binding site4171Substrate; for pectinesterase activity By similarity
Site3241Transition state stabilizer By similarity

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Disulfide bond339 ↔ 359 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3E989 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: C0A5DDE69CCE2BFE

FASTA51256,699
        10         20         30         40         50         60 
MGVIDMVLFW VLLVNALLIV DASSRNMPFA YQNEMQRHCS STKYTSLCVQ NLREFRHGSL 

        70         80         90        100        110        120 
DGLDFVSFLV NKTISDSNLL IPPLSSSMGS SKLVSLEDST YTLPSPSVSD SCERLMKMST 

       130        140        150        160        170        180 
RRLRQAMEAL NGSSRKRHTK HDVQTWLSAA MTFQQACKDS ILDSGGSSSA SAISHISQKM 

       190        200        210        220        230        240 
DHLSRLVSNS LTLVDTIMKN PKPKTKSTAL PRWVTAGERR LLVGRARAHV VVAKDGSGDY 

       250        260        270        280        290        300 
RTVMEAVTAA HGNGKDLTVI VGDDSATGGT SVPDTATMTV TGDGFIARDI GIKNIAGPRG 

       310        320        330        340        350        360 
HQAIALSITS DQSVLYRCSI SGYQDTLYAA ALRQFYRECD IYGTIDFIFG NAAAVFQSCN 

       370        380        390        400        410        420 
IFLRRPHGVK AYNVILANGR TDQRQNTGFA LHSCRIRTDS DLSPVKHKYS SYLGRPWRKY 

       430        440        450        460        470        480 
SRAIVMESYI DDAIAEGGWA GWLDSGDEVL KTLYFGEFKN YGPKARISKR VTWEGFHSIG 

       490        500        510 
FEEANYFSVV KRRNGEDVTN GFKYKFKIKI QI

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Pectin methylesterases: sequence-structural features and phylogenetic relationships."
Markovic O., Janecek S.
Carbohydr. Res. 339:2281-2295(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[4]"Comprehensive expression profiling of the pectin methylesterase gene family during silique development in Arabidopsis thaliana."
Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F., Guerineau F., Pelloux J.
Planta 224:782-791(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF296834 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92898.1.
IPIIPI00537895.
RefSeqNP_197586.1. NM_122093.1.
UniGeneAt.54935.

3D structure databases

ProteinModelPortalQ3E989.
SMRQ3E989. Positions 228-479.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT5G20860.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G20860.1; AT5G20860.1; AT5G20860.
GeneID832209.
KEGGath:AT5G20860.

Organism-specific databases

TAIRAt5g20860.

Phylogenomic databases

eggNOGCOG4677.
HOGENOMHOG000217409.
InParanoidQ3E989.
OMAQQACKDS.
PhylomeDBQ3E989.
ProtClustDBPLN02698.

Enzyme and pathway databases

UniPathwayUPA00545; UER00823.

Gene expression databases

GenevestigatorQ3E989.

Family and domain databases

Gene3D1.20.140.40. 1 hit.
2.160.20.10. 1 hit.
InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME54_ARATH
AccessionPrimary (citable) accession number: Q3E989
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: November 8, 2005
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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