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Reviewed, UniProtKB/Swiss-Prot Q9SG77 (PME24_ARATH)

Last modified November 3, 2009. Version 47. 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:
    Putative pectinesterase/pectinesterase inhibitor 24
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 24
        Alternative name(s):
            Pectin methylesterase inhibitor 24
    2- Recommended name:
            Pectinesterase 24
                Short name=PE 24
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 24
              Short name=AtPME24
Gene names
Name: PME24
Synonyms: ARATH24
Ordered Locus Names: At3g10710
ORF Names: T7M13.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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

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.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
   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: InterPro

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain1 – 561561Putative pectinesterase/pectinesterase inhibitor 24
PRO_0000370187

Regions

Transmembrane26 – 4621 Potential
Region64 – 211148Pectinesterase inhibitor 24
Region255 – 548294Pectinesterase 24

Sites

Active site3831Proton donor; for pectinesterase activity By similarity
Active site4041Nucleophile; for pectinesterase activity By similarity
Binding site3301Substrate; for pectinesterase activity By similarity
Binding site3601Substrate; for pectinesterase activity By similarity
Binding site4681Substrate; for pectinesterase activity By similarity
Binding site4701Substrate; for pectinesterase activity By similarity
Site3821Transition state stabilizer By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation4721N-linked (GlcNAc...) Potential
Disulfide bond397 ↔ 417 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9SG77-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 67136DD2C6AD074B

FASTA56162,103
        10         20         30         40         50         60 
MSSPYGKVDE REHVRLEARR KTRKNIAIIA VSLVILAGIV IGAVFGTMAH KKSPETVETN 

        70         80         90        100        110        120 
NNGDSISVSV KAVCDVTLHK EKCFETLGSA PNASSLNPEE LFRYAVKITI AEVSKAINAF 

       130        140        150        160        170        180 
SSSLGDEKNN ITMNACAELL DLTIDNLNNT LTSSSNGDVT VPELVDDLRT WLSSAGTYQR 

       190        200        210        220        230        240 
TCVETLAPDM RPFGESHLKN STELTSNALA IITWLGKIAD SFKLRRRLLT TADVEVDFHA 

       250        260        270        280        290        300 
GRRLLQSTDL RKVADIVVAK DGSGKYRTIK RALQDVPEKS EKRTIIYVKK GVYFENVKVE 

       310        320        330        340        350        360 
KKMWNVIVVG DGESKSIVSG RLNVIDGTPT FKTATFAVFG KGFMARDMGF INTAGPSKHQ 

       370        380        390        400        410        420 
AVALMVSADL TAFYRCTMNA YQDTLYVHAQ RQFYRECTII GTVDFIFGNS ASVLQSCRIL 

       430        440        450        460        470        480 
PRRPMKGQQN TITAQGRTDP NMNTGISIHR CNISPLGDLT DVMTFLGRPW KNFSTTVIMD 

       490        500        510        520        530        540 
SYLHGFIDRK GWLPWTGDSA PDTIFYGEYK NTGPGASTKN RVKWKGLRFL STKEANRFTV 

       550        560 
KPFIDGGRWL PATKVPFRSG L

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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]"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.

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Cross-references

Sequence databases

AC011708 Genomic DNA. Translation: AAF19578.1.
IPIIPI00547922.
RefSeqNP_187682.1.
UniGeneAt.53254

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBaseSearch...

Genome annotation databases

GeneID820240.
GenomeReviewsGene locus AT3G10710 in contig BA000014_GR.
KEGGath:AT3G10710.
NMPDRfig|3702.1.peg.13108.

Organism-specific databases

TAIRAt3g10710.

Phylogenomic databases

OMARECTIIG.

Gene expression databases

GenevestigatorQ9SG77.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
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]
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePME24_ARATH
AccessionPrimary (citable) accession number: Q9SG77
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 47 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