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Reviewed, UniProtKB/Swiss-Prot Q8VYZ3 (PME53_ARATH)

Last modified February 9, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable pectinesterase 53
      Short name=PE 53
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 53
      Short name=AtPME53
Gene names
Name: PME53
Synonyms: ARATH53
Ordered Locus Names: At5g19730
ORF Names: T29J13.150
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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

Sequence similarities

Belongs to the pectinesterase family.

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Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from direct assay. Source: TAIR

cytoplasm

Inferred from direct assay. Source: TAIR

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaspartyl esterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 383355Probable pectinesterase 53
PRO_0000371701

Sites

Active site2241Proton donor By similarity
Active site2451Nucleophile By similarity
Binding site1661Substrate By similarity
Binding site2011Substrate By similarity
Binding site3011Substrate By similarity
Binding site3031Substrate By similarity
Site2231Transition state stabilizer By similarity

Amino acid modifications

Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation1831N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q8VYZ3-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 3BA67E80D5301F21

FASTA38342,541
        10         20         30         40         50         60 
MPKLNSTQAP NLFLLLLVIL LCSTQTQCHT KGLRLRPRNQ KNMNTTSDRT QNPEDEFMKW 

        70         80         90        100        110        120 
VRFVGSLKHS VFKAAKNKLF PSYTLTVHKK SNKGDFTKIQ DAIDSLPLIN FVRVVIKVHA 

       130        140        150        160        170        180 
GVYKEKVSIP PLKAFITIEG EGAEKTTVEW GDTAQTPDSK GNPMGTYNSA SFAVNSPFFV 

       190        200        210        220        230        240 
AKNITFRNTT PVPLPGAVGK QAVALRVSAD NAAFFGCRML GAQDTLYDHL GRHYYKDCYI 

       250        260        270        280        290        300 
EGSVDFIFGN ALSLYEGCHV HAIADKLGAV TAQGRSSVLE DTGFSFVKCK VTGTGVLYLG 

       310        320        330        340        350        360 
RAWGPFSRVV FAYTYMDNII LPRGWYNWGD PSREMTVFYG QYKCTGAGAN YGGRVAWARE 

       370        380 
LTDEEAKPFL SLTFIDGSEW IKL

« Hide

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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: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Pectin methylesterases: sequence-structural features and phylogenetic relationships."
Markovic O., Janecek S.
Carbohydr. Res. 339:2281-2295(2004) [PubMed: 15337457] [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: 16622707] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF296838 Genomic DNA. No translation available.
AY065431 mRNA. Translation: AAL38872.1.
AY096559 mRNA. Translation: AAM20209.1.
IPIIPI00527343.
RefSeqNP_197474.1.
UniGeneAt.28487

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
SMRQ8VYZ3. Positions 83-382.
ModBaseSearch...

Genome annotation databases

GeneID832093.
GenomeReviewsGene locus AT5G19730 in contig BA000015_GR.
KEGGath:AT5G19730.
NMPDRfig|3702.1.peg.24174.

Organism-specific databases

TAIRAt5g19730.

Phylogenomic databases

eggNOGeuNOG09608.
HOGENOMHBG747179.
InParanoidQ8VYZ3.
OMAIDGSEWI.

Gene expression databases

ArrayExpressQ8VYZ3.
GenevestigatorQ8VYZ3.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME53_ARATH
AccessionPrimary (citable) accession number: Q8VYZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2002
Last modified: February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents