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Reviewed, UniProtKB/Swiss-Prot Q9LY19 (PME48_ARATH)

Last modified October 13, 2009. Version 31. 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

Names and origin

Protein namesRecommended name:
    Probable pectinesterase 48
      Short name=PE 48
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 48
      Short name=AtPME48
Gene names
Name: PME48
Synonyms: ARATH48
Ordered Locus Names: At5g07410
ORF Names: T2I1.120
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length361 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

Secretedcell wall By similarity.

Tissue specificity

Expressed in mature pollen grains in the anthers and on the stigma. Found in pollen tubes within the style. Ref.5

Sequence similarities

Belongs to the pectinesterase family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   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

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 361338Probable pectinesterase 48
PRO_0000371696

Sites

Active site1971Proton donor By similarity
Active site2181Nucleophile By similarity
Binding site1741Substrate By similarity
Binding site2751Substrate By similarity
Binding site2771Substrate By similarity
Site1961Transition state stabilizer By similarity

Experimental info

Sequence conflict481A → V in AAM65347. Ref.2
Sequence conflict1001H → P in AAM65347. Ref.2
Sequence conflict2541K → N in AAM65347. Ref.2
Sequence conflict2701G → V in AAM65347. Ref.2
Sequence conflict3421C → R in AAM65347. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9LY19-1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: C0663F0A5FAB2D3E

FASTA36139,337
        10         20         30         40         50         60 
MRYTNVSILL GMLVIFVSPM VFADDLTPIP EGKPQVVQWF NTHVGPLAQR KGLDPALVAA 

        70         80         90        100        110        120 
EAAPRIINVN PKGGEFKTLT DAIKSVPAGN TKRVIIKMAH GEYREKVTID RNKPFITLMG 

       130        140        150        160        170        180 
QPNAMPVITY DGTAAKYGTV DSASLIILSD YFMAVNIVVK NTAPAPDGKT KGAQALSMRI 

       190        200        210        220        230        240 
SGNFAAFYNC KFYGFQDTIC DDTGNHFFKD CYVEGTFDFI FGSGTSMYLG TQLHVVGDGI 

       250        260        270        280        290        300 
RVIAAHAGKS AEEKSGYSFV HCKVTGTGGG IYLGRAWMSH PKVVYAYTEM TSVVNPTGWQ 

       310        320        330        340        350        360 
ENKTPAHDKT VFYGEYKCSG PGSHKAKRVP FTQDIDDKEA NCFLSLGYIQ GSKWLLPPPA 


L 

« 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: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-361.
Strain: cv. Columbia.
[4]"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.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

AL163912 Genomic DNA. Translation: CAB87930.1. Different initiation.
AY087811 mRNA. Translation: AAM65347.1. Different initiation.
AK221986 mRNA. Translation: BAD94545.1. Different initiation.
IPIIPI00545321.
PIRT49880.
RefSeqNP_568181.1.

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9LY19.

Genome annotation databases

GeneID830632.
GenomeReviewsGene locus AT5G07410 in contig BA000015_GR.
NMPDRfig|3702.1.peg.22881.

Organism-specific databases

GeneFarm502. 8.
TAIRAt5g07410.

Gene expression databases

GenevestigatorQ9LY19.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME48_ARATH
AccessionPrimary (citable) accession number: Q9LY19
Secondary accession number(s): Q56WP9, Q8LAH3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: October 13, 2009
This is version 31 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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