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Q8GXA1 (PME23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. Feed History...

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

Protein namesRecommended name:
Probable pectinesterase/pectinesterase inhibitor 23

Including the following 2 domains:

  1. Pectinesterase inhibitor 23
    Alternative name(s):
    Pectin methylesterase inhibitor 23
  2. Pectinesterase 23
    Short name=PE 23
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 23
    Short name=AtPME23
Gene names
Name:PME23
Synonyms:ARATH23
Ordered Locus Names:At3g06830
ORF Names:F3E22.3
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length568 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.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 caution

The sequence AAF63815.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 568535Probable pectinesterase/pectinesterase inhibitor 23
PRO_0000371679

Regions

Region45 – 198154Pectinesterase inhibitor 23
Region251 – 548298Pectinesterase 23

Sites

Active site3861Proton donor; for pectinesterase activity By similarity
Active site4071Nucleophile; for pectinesterase activity By similarity
Binding site3331Substrate; for pectinesterase activity By similarity
Binding site3631Substrate; for pectinesterase activity By similarity
Binding site4751Substrate; for pectinesterase activity By similarity
Binding site4771Substrate; for pectinesterase activity By similarity
Site3851Transition state stabilizer By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Disulfide bond400 ↔ 420 By similarity

Experimental info

Sequence conflict1071K → E in BAC42959. Ref.3
Sequence conflict5681V → A in BAC42959. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8GXA1 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: FE92C797055361A7

FASTA56861,886
        10         20         30         40         50         60 
MGSDGDKKKK FIVAGSVSGF LVIMVVSVAV VTSKHSPKDD ENHIRKTTKA VQAVCAPTDF 

        70         80         90        100        110        120 
KDTCVNSLMG ASPDSDDPVD LIKLGFKVTI KSINESLEKA SGDIKAKADK NPEAKGAFEL 

       130        140        150        160        170        180 
CEKLMIDAID DLKKCMDHGF SVDQIEVFVE DLRVWLSGSI AFQQTCMDSF GEIKSNLMQD 

       190        200        210        220        230        240 
MLKIFKTSRE LSSNSLAMVT RISTLIPNSN LTGLTGALAK YARKLLSTED SIPTWVGPEA 

       250        260        270        280        290        300 
RRLMAAQGGG PGPVKANAVV AQDGTGQFKT ITDALNAVPK GNKVPFIIHI KEGIYKEKVT 

       310        320        330        340        350        360 
VTKKMPHVTF IGDGPNKTLI TGSLNFGIGK VKTFLTATIT IEGDHFTAKN IGIENTAGPE 

       370        380        390        400        410        420 
GGQAVALRVS ADYAVFHSCQ IDGHQDTLYV HSHRQFYRDC TVSGTVDFIF GDAKCILQNC 

       430        440        450        460        470        480 
KIVVRKPNKG QTCMVTAQGR SNVRESTGLV LHGCHITGDP AYIPMKSVNK AYLGRPWKEF 

       490        500        510        520        530        540 
SRTIIMKTTI DDVIDPAGWL PWSGDFALKT LYYAEHMNTG PGSNQAQRVK WPGIKKLTPQ 

       550        560 
DALLYTGDRF LRGDTWIPQT QVPYTAKV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Arabidopsis ORF clones."
Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.
Submitted (MAR-2007) 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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC023912 Genomic DNA. Translation: AAF63815.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74464.1.
AK118345 mRNA. Translation: BAC42959.2.
BT030353 mRNA. Translation: ABO38766.1.
IPIIPI00523955.
RefSeqNP_187339.2. NM_111563.3.
UniGeneAt.40454.

3D structure databases

HSSPHSSP built from PDB template 1XG2 based on UniProtKB P14280.
ProteinModelPortalQ8GXA1.
SMRQ8GXA1. Positions 254-568.
ModBaseSearch...

Proteomic databases

PRIDEQ8GXA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G06830.1; AT3G06830.1; AT3G06830.
GeneID819867.
GenomeReviewsGene locus AT3G06830 in contig BA000014_GR.
KEGGath:AT3G06830.

Organism-specific databases

GeneFarm484. 8.
TAIRAt3g06830.

Phylogenomic databases

eggNOGCOG4677.
GeneTreeEPGT00070000028024.
HOGENOMHBG747179.
OMANIGIENT.
PhylomeDBQ8GXA1.
ProtClustDBPLN02990.

Enzyme and pathway databases

BRENDA3.1.1.11. 399.

Gene expression databases

GenevestigatorQ8GXA1.

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. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME23_ARATH
AccessionPrimary (citable) accession number: Q8GXA1
Secondary accession number(s): A4FVQ5, Q9M7Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 54 of the entry and version 3 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