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Reviewed, UniProtKB/Swiss-Prot Q9FHN5 (PME59_ARATH)

Last modified February 9, 2010. Version 48. 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 59
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 59
        Alternative name(s):
            Pectin methylesterase inhibitor 59
    2- Recommended name:
            Pectinesterase 59
                Short name=PE 59
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 59
              Short name=AtPME59
Gene names
Name: PME59
Synonyms: ARATH59
Ordered Locus Names: At5g51490
ORF Names: K17N15.4
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 length536 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.3

Developmental stage

Expressed during late developmental phases of siliques. Ref.3

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
   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: 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 – 3030 Potential
Chain31 – 536506Probable pectinesterase/pectinesterase inhibitor 59
PRO_0000370180

Regions

Region31 – 183153Pectinesterase inhibitor 59
Region221 – 522302Pectinesterase 59

Sites

Active site3511Proton donor; for pectinesterase activity By similarity
Active site3721Nucleophile; for pectinesterase activity By similarity
Binding site2981Substrate; for pectinesterase activity By similarity
Binding site3281Substrate; for pectinesterase activity By similarity
Binding site4401Substrate; for pectinesterase activity By similarity
Binding site4421Substrate; for pectinesterase activity By similarity
Site3501Transition state stabilizer By similarity

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Disulfide bond365 ↔ 385 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9FHN5-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 17FBC0F027F35BF9

FASTA53658,868
        10         20         30         40         50         60 
MNMMMQKLSI LFLHLILLVL LCVHPLTTVA DRNSTDWCDK TPYPDPCKCY FKNHNGFQQP 

        70         80         90        100        110        120 
TQLSEFRVML VEAAMDRAIS ARAELTNSGK NCTDSKKQAV LADCIDLYGD TIMQLNRTLH 

       130        140        150        160        170        180 
GVSPKAGAAK SCTDFDAQTW LSTALTNTET CRRGSSDLNV TDFITPIVSN TKISHLISNC 

       190        200        210        220        230        240 
LAVNGALLTA GNKGNTTANQ KGFPTWLSRK DKRLLRAVRA NLVVAKDGSG HFNTVQAAID 

       250        260        270        280        290        300 
VAGRRKVTSG RFVIYVKRGI YQENINVRLN NDDIMLVGDG MRSTIITGGR SVQGGYTTYN 

       310        320        330        340        350        360 
SATAGIEGLH FIAKGITFRN TAGPAKGQAV ALRSSSDLSI FYKCSIEGYQ DTLMVHSQRQ 

       370        380        390        400        410        420 
FYRECYIYGT VDFIFGNAAA VFQNCLILPR RPLKGQANVI TAQGRADPFQ NTGISIHNSR 

       430        440        450        460        470        480 
ILPAPDLKPV VGTVKTYMGR PWMKFSRTVV LQTYLDNVVS PVGWSPWIEG SVFGLDTLFY 

       490        500        510        520        530 
AEYKNTGPAS STRWRVSWKG FHVLGRASDA SAFTVGKFIA GTAWLPRTGI PFTSGL

« Hide

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References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"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		AB018109 Genomic DNA. Translation: BAB08665.1.
IPIIPI00519924.
RefSeqNP_199962.1.
UniGeneAt.7804

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
SMRQ9FHN5. Positions 35-188, 216-536.
ModBaseSearch...

Proteomic databases

PRIDEQ9FHN5.

Genome annotation databases

GeneID835223.
GenomeReviewsGene locus AT5G51490 in contig BA000015_GR.
KEGGath:AT5G51490.
NMPDRfig|3702.1.peg.27019.

Organism-specific databases

GeneFarm303. 8.
TAIRAt5g51490.

Phylogenomic databases

eggNOGCOG4677.
HOGENOMHBG747179.
InParanoidQ9FHN5.
OMASIHNSRI.

Gene expression databases

GenevestigatorQ9FHN5.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
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]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME59_ARATH
AccessionPrimary (citable) accession number: Q9FHN5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 48 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