Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9LUL8 (PME26_ARATH)

Last modified October 13, 2009. Version 47. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Putative pectinesterase/pectinesterase inhibitor 26
Alternative name(s):
    AtPMEpcrC
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 26
        Alternative name(s):
            Pectin methylesterase inhibitor 26
    2- Recommended name:
            Pectinesterase 26
                Short name=PE 26
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 26
              Short name=AtPME26
Gene names
Name: PME26
Synonyms: ARATH26
Ordered Locus Names: At3g14300
ORF Names: MLN21.8
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

Hide | Top

Protein attributes

Sequence length968 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

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

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in flowers. Ref.2

Miscellaneous

The PMEI regions may act as autoinhibitory domains 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.

Hide | Top

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionAspartyl esterase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from electronic annotation. Source: InterPro

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 968968Putative pectinesterase/pectinesterase inhibitor 26
PRO_0000370189

Regions

Transmembrane33 – 5321 Potential
Region71 – 230160Pectinesterase inhibitor 26 A
Region265 – 430166Pectinesterase inhibitor 26 B
Region453 – 614162Pectinesterase inhibitor 26 C
Region660 – 954295Pectinesterase 26

Sites

Active site7881Proton donor; for pectinesterase activity By similarity
Active site8091Nucleophile; for pectinesterase activity By similarity
Binding site7351Substrate; for pectinesterase activity By similarity
Binding site7651Substrate; for pectinesterase activity By similarity
Binding site8721Substrate; for pectinesterase activity By similarity
Binding site8741Substrate; for pectinesterase activity By similarity
Site7871Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation5411N-linked (GlcNAc...) Potential
Glycosylation5591N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Glycosylation7371N-linked (GlcNAc...) Potential
Glycosylation8631N-linked (GlcNAc...) Potential
Glycosylation9001N-linked (GlcNAc...) Potential
Disulfide bond802 ↔ 822 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9LUL8-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 96DB0EAFAFA43898

FASTA968105,628
        10         20         30         40         50         60 
MDTVKSINKG YGKVDETQDL ALKRKTRKRL YQIGISVAVL VAIIISSTVT IAIHSRKGNS 

        70         80         90        100        110        120 
PHPTPSSVPE LTPAASLKTV CSVTNYPVSC FSSISKLPLS NTTDPEVIFR LSLQVVIDEL 

       130        140        150        160        170        180 
NSIVELPKKL AEETDDEGLK SALSVCEHLL DLAIDRVNET VSAMEVVDGK KILNAATIDD 

       190        200        210        220        230        240 
LLTWLSAAVT YHGTCLDALD EISHTNSAIP LKLKSGMVNS TEFTSNSLAI VAKILSTISD 

       250        260        270        280        290        300 
FGIPIHGRRL LNSSPHATPI SVPKLTPAAS LRNVCSVTRY PASCVSSISK LPSSNTTDPE 

       310        320        330        340        350        360 
ALFRLSLQVV INELNSIAGL PKKLAEETDD ERLKSSLSVC GDVFNDAIDI VNDTISTMEE 

       370        380        390        400        410        420 
VGDGKKILKS STIDEIQTWL SAAVTDHDTC LDALDELSQN KTEYANSPIS LKLKSAMVNS 

       430        440        450        460        470        480 
RKFTSNSLAI IAKFPIHERH GVQSPRLRKS PHPTPSSVLR TVCNVTNYPA SCISSISKLP 

       490        500        510        520        530        540 
LSKTTTDPKV LFRLSLQVTF DELNSIVGLP KKLAEETNDE GLKSALSVCA DVFDLAVDSV 

       550        560        570        580        590        600 
NDTISSLDEV ISGGKKNLNS STIGDLITWL SSAVTDIGTC GDTLDEDNYN SPIPQKLKSA 

       610        620        630        640        650        660 
MVNSTEFTSN SLAIVAQVLK KPSKSRIPVQ GRRLLNSNSF PNWVRPGVRR LLQAKNLTPH 

       670        680        690        700        710        720 
VTVAADGSGD VRTVNEAVWR VPKKGKTMFV IYVKAGTYVE NVLMKKDKWN VFIYGDGRDK 

       730        740        750        760        770        780 
TIISGSTNMV DGVRTFNTST FATEGKGFMM KDMGIINTAG PEKHQAVAFR SDSDRSVYYR 

       790        800        810        820        830        840 
CSFDGYQDTL YTHSNRQYYR NCDVTGTVDF IFGAGTVVFQ GCSIRPRQPL PNQFNTITAE 

       850        860        870        880        890        900 
GTQEANQNTG ISIHQCTISP NGNVTATTYL GRPWKLFSKT VIMQSVIGSF VNPAGWIAWN 

       910        920        930        940        950        960 
STYDPPPRTI FYREYKNSGP GSDLSKRVKW AGYKPISSDD EAARFTVKYF LRGDDNWIPK 


AVMGMPPL

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Characterization of the pectin methylesterase-like gene AtPME3: a new member of a gene family comprising at least 12 genes in Arabidopsis thaliana."
Micheli F., Holliger C., Goldberg R., Richard L.
Gene 220:13-20(1998) [PubMed: 9767082] [Abstract]
Cited for: TISSUE SPECIFICITY.
[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.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AB022220 Genomic DNA. Translation: BAB01036.1.
IPIIPI00538572.
RefSeqNP_188047.1.
UniGeneAt.53309

3D structure databases

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

Genome annotation databases

GeneID820650.
GenomeReviewsGene locus AT3G14300 in contig BA000014_GR.
KEGGath:AT3G14300.
NMPDRfig|3702.1.peg.13563.

Organism-specific databases

GeneFarm415. 8.
TAIRAt3g14300.

Gene expression databases

GenevestigatorQ9LUL8.

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. 3 hits.
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 3 hits.
[Graphical view]
TIGRFAMsTIGR01614. PME_inhib. 3 hits.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry namePME26_ARATH
AccessionPrimary (citable) accession number: Q9LUL8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 1, 2000
Last modified: October 13, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

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