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Q9FK05 (PME61_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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 61

Including the following 2 domains:

  1. Pectinesterase inhibitor 61
    Alternative name(s):
    Pectin methylesterase inhibitor 61
  2. Pectinesterase 61
    Short name=PE 61
    EC=3.1.1.11
    Alternative name(s):
    AtPMEpcrF
    Pectin methylesterase 61
    Short name=AtPME61
Gene names
Name:PME61
Synonyms:ARATH61
Ordered Locus Names:At5g53370
ORF Names:K19E1.17
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in siliques, floral stems and rosettes leaves. Ref.4 Ref.6

Developmental stage

Expressed throughout silique development. 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

Chain1 – 587587Probable pectinesterase/pectinesterase inhibitor 61
PRO_0000371707

Regions

Transmembrane35 – 5521Helical; Potential
Region69 – 223155Pectinesterase inhibitor 61
Region273 – 571299Pectinesterase 61

Sites

Active site4021Proton donor; for pectinesterase activity By similarity
Active site4231Nucleophile; for pectinesterase activity By similarity
Binding site3491Substrate; for pectinesterase activity By similarity
Binding site3791Substrate; for pectinesterase activity By similarity
Binding site4911Substrate; for pectinesterase activity By similarity
Binding site4931Substrate; for pectinesterase activity By similarity
Site4011Transition state stabilizer By similarity

Amino acid modifications

Modified residue5391Phosphoserine Ref.7
Disulfide bond416 ↔ 436 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9FK05 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A60B9271DE489DBD

FASTA58764,241
        10         20         30         40         50         60 
MGYDRLGPSG PSNPNQKDPA TSLPELQKKT KTKLILFTLA VLVVGVVCFG IFAGIRAVDS 

        70         80         90        100        110        120 
GKTEPKLTRK PTQAISRTCS KSLYPNLCID TLLDFPGSLT ADENELIHIS FNATLQKFSK 

       130        140        150        160        170        180 
ALYTSSTITY TQMPPRVRSA YDSCLELLDD SVDALTRALS SVVVVSGDES HSDVMTWLSS 

       190        200        210        220        230        240 
AMTNHDTCTD GFDEIEGQGG EVKDQVIGAV KDLSEMVSNC LAIFAGKVKD LSGVPVVNNR 

       250        260        270        280        290        300 
KLLGTEETEE LPNWLKREDR ELLGTPTSAI QADITVSKDG SGTFKTIAEA IKKAPEHSSR 

       310        320        330        340        350        360 
RFVIYVKAGR YEEENLKVGR KKTNLMFIGD GKGKTVITGG KSIADDLTTF HTATFAATGA 

       370        380        390        400        410        420 
GFIVRDMTFE NYAGPAKHQA VALRVGGDHA VVYRCNIIGY QDALYVHSNR QFFRECEIYG 

       430        440        450        460        470        480 
TVDFIFGNAA VILQSCNIYA RKPMAQQKIT ITAQNRKDPN QNTGISIHAC KLLATPDLEA 

       490        500        510        520        530        540 
SKGSYPTYLG RPWKLYSRVV YMMSDMGDHI DPRGWLEWNG PFALDSLYYG EYMNKGLGSG 

       550        560        570        580 
IGQRVKWPGY HVITSTVEAS KFTVAQFISG SSWLPSTGVS FFSGLSQ 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed: 9734815] [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]"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.
[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.
[7]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013388 Genomic DNA. Translation: BAB09799.1.
CP002688 Genomic DNA. Translation: AED96345.1.
AF360340 mRNA. Translation: AAK28637.1.
AY051077 mRNA. Translation: AAK93754.1.
IPIIPI00530003.
RefSeqNP_200149.1. NM_124716.2.
UniGeneAt.24561.
At.29558.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortalQ9FK05.
SMRQ9FK05. Positions 72-226, 268-585.
ModBaseSearch...

Proteomic databases

PRIDEQ9FK05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G53370.1; AT5G53370.1; AT5G53370.
GeneID835418.
GenomeReviewsGene locus AT5G53370 in contig BA000015_GR.
KEGGath:AT5G53370.
NMPDRfig|3702.1.peg.27231.

Organism-specific databases

GeneFarm298. 8.
TAIRAt5g53370.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000027901.
HOGENOMHBG747179.
InParanoidQ9FK05.
OMARVVYMMS.
PhylomeDBQ9FK05.
ProtClustDBPLN02484.

Gene expression databases

ArrayExpressQ9FK05.
GenevestigatorQ9FK05.

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]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME61_ARATH
AccessionPrimary (citable) accession number: Q9FK05
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 61 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