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Reviewed, UniProtKB/Swiss-Prot O81415 (PME39_ARATH)

Last modified October 13, 2009. Version 52. 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/pectinesterase inhibitor 39
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 39
        Alternative name(s):
            Pectin methylesterase inhibitor 39
    2- Recommended name:
            Pectinesterase 39
                Short name=PE 39
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 39
              Short name=AtPME39
Gene names
Name: PME39
Synonyms: ARATH39
Ordered Locus Names: At4g02300
ORF Names: T2H3.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length532 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 but not in flower buds. Ref.4

Developmental stage

Expression restricted to early to mid-stage of silique development. 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.

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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 electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaspartyl esterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme inhibitor activity

Inferred from electronic annotation. Source: InterPro

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 – 3434 Potential
Chain35 – 532498Probable pectinesterase/pectinesterase inhibitor 39
PRO_0000371689

Regions

Region35 – 169135Pectinesterase inhibitor 39
Region221 – 518298Pectinesterase 39

Sites

Active site3491Proton donor; for pectinesterase activity By similarity
Active site3701Nucleophile; for pectinesterase activity By similarity
Binding site2961Substrate; for pectinesterase activity By similarity
Binding site3261Substrate; for pectinesterase activity By similarity
Binding site4381Substrate; for pectinesterase activity By similarity
Binding site4401Substrate; for pectinesterase activity By similarity
Site3481Transition state stabilizer By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation2211N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
O81415-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 58513200794D3D17

FASTA53259,824
        10         20         30         40         50         60 
MINNHPIREK PKHIIFNLLS LIFFLIFLST VVSSQSPSYT THKTQRLTET KTIPELIIAD 

        70         80         90        100        110        120 
LNLTILKVNL ASSNFSDLQT RLFPNLTHYE RCAFEDCLGL LDDTISDLET AVSDLRSSSL 

       130        140        150        160        170        180 
EFNDISMLLT NVMTYQDTCL DGFSTSDNEN NNDMTYELPE NLKEIILDIS NNLSNSLHML 

       190        200        210        220        230        240 
QVISRKKPSP KSSEVDVEYP SWLSENDQRL LEAPVQETNY NLSVAIDGTG NFTTINDAVF 

       250        260        270        280        290        300 
AAPNMSETRF IIYIKGGEYF ENVELPKKKT MIMFIGDGIG KTVIKANRSR IDGWSTFQTP 

       310        320        330        340        350        360 
TVGVKGKGYI AKDISFVNSA GPAKAQAVAF RSGSDHSAFY RCEFDGYQDT LYVHSAKQFY 

       370        380        390        400        410        420 
RECDIYGTID FIFGNAAVVF QNSSLYARKP NPGHKIAFTA QSRNQSDQPT GISILNCRIL 

       430        440        450        460        470        480 
AAPDLIPVKE NFKAYLGRPW RKYSRTVIIK SFIDDLIHPA GWLEGKKDFA LETLYYGEYM 

       490        500        510        520        530 
NEGPGANMAK RVTWPGFRRI ENQTEATQFT VGPFIDGSTW LNSTGIPFSL GF

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., Redman J.C., Wu H.C., Utterback T., Town C.D.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
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.

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Cross-references

Sequence databases

AF075597 Genomic DNA. Translation: AAC28174.1.
AL161494 Genomic DNA. Translation: CAB80723.1.
DQ056637 mRNA. Translation: AAY78785.1.
IPIIPI00524286.
PIRT01418.
RefSeqNP_192139.1.
UniGeneAt.54096

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBaseSearch...

Genome annotation databases

GeneID827708.
GenomeReviewsGene locus AT4G02300 in contig CT486007_GR.
KEGGath:AT4G02300.
NMPDRfig|3702.1.peg.18040.

Organism-specific databases

GeneFarm333. 8.
TAIRAt4g02300.

Gene expression databases

ArrayExpressO81415.
GenevestigatorO81415.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME39_ARATH
AccessionPrimary (citable) accession number: O81415
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: November 1, 1998
Last modified: October 13, 2009
This is version 52 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