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Q9FJ21 (PME58_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pectinesterase/pectinesterase inhibitor 58

Including the following 2 domains:

  1. Pectinesterase inhibitor 58
    Alternative name(s):
    Pectin methylesterase inhibitor 58
  2. Pectinesterase 58
    Short name=PE 58
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 58
    Short name=AtPME58
Gene names
Name:PME58
Synonyms:ARATH58
Ordered Locus Names:At5g49180
ORF Names:K21P3.5
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length571 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

Secreted › cell wall By similarity.

Tissue specificity

Expressed in siliques, but not in flower buds. Ref.6

Developmental stage

Expression restricted to early to mid-stage of silique development. Not found in vegetative stage. Expressed in the micropyle area of the ovule just after fertilization. Ref.6

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 571543Probable pectinesterase/pectinesterase inhibitor 58
PRO_0000371706

Regions

Region49 – 204156Pectinesterase inhibitor 58
Region259 – 556298Pectinesterase 58

Sites

Active site3881Proton donor; for pectinesterase activity By similarity
Active site4091Nucleophile; for pectinesterase activity By similarity
Binding site3351Substrate; for pectinesterase activity By similarity
Binding site3651Substrate; for pectinesterase activity By similarity
Binding site4771Substrate; for pectinesterase activity By similarity
Binding site4791Substrate; for pectinesterase activity By similarity
Site3871Transition state stabilizer By similarity

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Disulfide bond402 ↔ 422 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9FJ21 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 777402570880BBC9

FASTA57162,799
        10         20         30         40         50         60 
MGVDGELKKK KCIIAGVITA LLVLMVVAVG ITTSRNTSHS EKIVPVQIKT ATTAVEAVCA 

        70         80         90        100        110        120 
PTDYKETCVN SLMKASPDST QPLDLIKLGF NVTIRSIEDS IKKASVELTA KAANDKDTKG 

       130        140        150        160        170        180 
ALELCEKLMN DATDDLKKCL DNFDGFSIPQ IEDFVEDLRV WLSGSIAYQQ TCMDTFEETN 

       190        200        210        220        230        240 
SKLSQDMQKI FKTSRELTSN GLAMITNISN LLGEFNVTGV TGDLGKYARK LLSAEDGIPS 

       250        260        270        280        290        300 
WVGPNTRRLM ATKGGVKANV VVAHDGSGQY KTINEALNAV PKANQKPFVI YIKQGVYNEK 

       310        320        330        340        350        360 
VDVTKKMTHV TFIGDGPTKT KITGSLNYYI GKVKTYLTAT VAINGDNFTA KNIGFENTAG 

       370        380        390        400        410        420 
PEGHQAVALR VSADLAVFYN CQIDGYQDTL YVHSHRQFFR DCTVSGTVDF IFGDGIVVLQ 

       430        440        450        460        470        480 
NCNIVVRKPM KSQSCMITAQ GRSDKRESTG LVLQNCHITG EPAYIPVKSI NKAYLGRPWK 

       490        500        510        520        530        540 
EFSRTIIMGT TIDDVIDPAG WLPWNGDFAL NTLYYAEYEN NGPGSNQAQR VKWPGIKKLS 

       550        560        570 
PKQALRFTPA RFLRGNLWIP PNRVPYMGNF Q

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
DNA Res. 5:379-391(1998) [PubMed: 10048488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"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].
[5]"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.
[6]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB016872 Genomic DNA. Translation: BAB10336.1.
CP002688 Genomic DNA. Translation: AED95779.1.
AY075680 mRNA. Translation: AAL77687.1.
BT002211 mRNA. Translation: AAN72223.1.
AY088442 mRNA. Translation: AAM65978.1.
IPIIPI00518436.
RefSeqNP_199729.1. NM_124295.2.
UniGeneAt.27750.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortalQ9FJ21.
SMRQ9FJ21. Positions 255-570.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9FJ21.

Proteomic databases

PRIDEQ9FJ21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G49180.1; AT5G49180.1; AT5G49180.
GeneID834977.
GenomeReviewsGene locus AT5G49180 in contig BA000015_GR.
KEGGath:AT5G49180.
NMPDRfig|3702.1.peg.26757.

Organism-specific databases

GeneFarm205. 8.
TAIRAt5g49180.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000028024.
HOGENOMHBG747179.
InParanoidQ9FJ21.
OMASINKAYL.
PhylomeDBQ9FJ21.
ProtClustDBPLN02990.

Gene expression databases

GenevestigatorQ9FJ21.

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.
KOK01051.
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME58_ARATH
AccessionPrimary (citable) accession number: Q9FJ21
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

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