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Q9FF78 (PME46_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 59. 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 46

Including the following 2 domains:

  1. Pectinesterase inhibitor 46
    Alternative name(s):
    Pectin methylesterase inhibitor 46
  2. Pectinesterase 46
    Short name=PE 46
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 46
    Short name=AtPME46
Gene names
Name:PME46
Synonyms:ARATH46
Ordered Locus Names:At5g04960
ORF Names:MUG13.18
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 length564 AA.
Sequence statusComplete.
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

Membrane; Single-pass membrane protein Potential.

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 – 564564Probable pectinesterase/pectinesterase inhibitor 46
PRO_0000370188

Regions

Transmembrane25 – 4521Helical; Potential
Region62 – 207146Pectinesterase inhibitor 46
Region257 – 550294Pectinesterase 46
Compositional bias221 – 2244Poly-Arg

Sites

Active site3851Proton donor; for pectinesterase activity By similarity
Active site4061Nucleophile; for pectinesterase activity By similarity
Binding site3321Substrate; for pectinesterase activity By similarity
Binding site3621Substrate; for pectinesterase activity By similarity
Binding site4701Substrate; for pectinesterase activity By similarity
Binding site4721Substrate; for pectinesterase activity By similarity
Site3841Transition state stabilizer By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Disulfide bond399 ↔ 419 By similarity

Experimental info

Sequence conflict4641I → T in AAO42295. Ref.3
Sequence conflict4691G → D in AAO42295. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9FF78 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0D3318722F2C0B99

FASTA56462,170
        10         20         30         40         50         60 
MSSYGRLDEH EQAKLEASRK TKKRIAIIAI SSIVLVCIVV GAVVGTTARD NSKKPPTENN 

        70         80         90        100        110        120 
GEPISVSVKA LCDVTLHKEK CFETLGSAPN ASRSSPEELF KYAVKVTITE LSKVLDGFSN 

       130        140        150        160        170        180 
GEHMDNATSA AMGACVELIG LAVDQLNETM TSSLKNFDDL RTWLSSVGTY QETCMDALVE 

       190        200        210        220        230        240 
ANKPSLTTFG ENHLKNSTEM TSNALAIITW LGKIADTVKF RRRRLLETGN AKVVVADLPM 

       250        260        270        280        290        300 
MEGRRLLESG DLKKKATIVV AKDGSGKYRT IGEALAEVEE KNEKPTIIYV KKGVYLENVR 

       310        320        330        340        350        360 
VEKTKWNVVM VGDGQSKTIV SAGLNFIDGT PTFETATFAV FGKGFMARDM GFINTAGPAK 

       370        380        390        400        410        420 
HQAVALMVSA DLSVFYKCTM DAFQDTMYAH AQRQFYRDCV ILGTVDFIFG NAAVVFQKCE 

       430        440        450        460        470        480 
ILPRRPMKGQ QNTITAQGRK DPNQNTGISI HNCTIKPLDN LTDIQTFLGR PWKDFSTTVI 

       490        500        510        520        530        540 
MKSFMDKFIN PKGWLPWTGD TAPDTIFYAE YLNSGPGAST KNRVKWQGLK TSLTKKEANK 

       550        560 
FTVKPFIDGN NWLPATKVPF NSDF

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed: 9330910] [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]"Arabidopsis ORF clones."
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB005245 Genomic DNA. Translation: BAB11518.1.
CP002688 Genomic DNA. Translation: AED90809.1.
BT004297 mRNA. Translation: AAO42295.1.
BT020587 mRNA. Translation: AAW80860.1.
IPIIPI00539417.
RefSeqNP_196115.1. NM_120578.4.
UniGeneAt.43216.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortalQ9FF78.
SMRQ9FF78. Positions 253-564.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9FF78.

Proteomic databases

PRIDEQ9FF78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G04960.1; AT5G04960.1; AT5G04960.
GeneID830378.
GenomeReviewsGene locus AT5G04960 in contig BA000015_GR.
KEGGath:AT5G04960.
NMPDRfig|3702.1.peg.22595.

Organism-specific databases

GeneFarm193. 8.
TAIRAt5g04960.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000028024.
InParanoidQ9FF78.
OMACEILPRR.
PhylomeDBQ9FF78.
ProtClustDBPLN02468.

Gene expression databases

GenevestigatorQ9FF78.

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 namePME46_ARATH
AccessionPrimary (citable) accession number: Q9FF78
Secondary accession number(s): Q84W31
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 59 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents