O04953 (PME52_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative pectinesterase 52
Short name=PE 52
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase 52
Short name=AtPME52

Gene names

Name:	PME52
Synonyms:	ARATH52
Ordered Locus Names:	At5g26810
ORF Names:	F2P16.5

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.4
Developmental stage	Expressed during late developmental phases of siliques. Ref.4
Sequence similarities	Belongs to the pectinesterase family.
Sequence caution	The sequence AAB61046.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW pectinesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 293	272	Putative pectinesterase 52		PRO_0000371700
Sites
	Active site	123	1	Proton donor By similarity
	Active site	144	1	Nucleophile By similarity
	Binding site	81	1	Substrate By similarity
	Binding site	206	1	Substrate By similarity
	Site	122	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	160	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O04953 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 917A69C10E7453F8	FASTA	293	32,350
	10 20 30 40 50 60 MPCLFIFIAL LLSSCIGTLK ALDQTCGNKV VNTIVVDQAG SGEGQRVTTI TYNGHAATDV 70 80 90 100 110 120 SSTFTSYPSH IVVRNLSIMN TYNRLTSLTK ANGMSWDIKP AVAISVYGDK SAFYNCDFLG 130 140 150 160 170 180 LQDTVWDNLG RHHFKNCYIE GAIDFIFGSG QSVYEDCHIN ATAGALASKV SFGYITAQGR 190 200 210 220 230 240 SSDSDPSGFV FLRGSVSGST SVYLGRAYGP FSRVIFIQTD LSSVVHPEGW YSWHYGGYEM 250 260 270 280 290 SFTYAEVECK GAGSDMSRRV PWIDKLHSFY TKQQFSISNF IDQDQWISNI PRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [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]	"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.
[4]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF007270 Genomic DNA. Translation: AAB61046.1. Sequence problems. CP002688 Genomic DNA. Translation: AED93608.1.
IPI	IPI00537186.
PIR	T01761.
RefSeq	NP_198033.2. NM_122563.2.
UniGene	At.55025.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	O04953.
SMR	O04953. Positions 6-290.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G26810.1; AT5G26810.1; AT5G26810.
GeneID	832739.
GenomeReviews	Gene locus AT5G26810 in contig BA000015_GR.
KEGG	ath:AT5G26810.
Organism-specific databases
TAIR	At5g26810.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000032090.
HOGENOM	HBG747179.
OMA	CHINATA.
PhylomeDB	O04953.
ProtClustDB	CLSN2917839.
Gene expression databases
Genevestigator	O04953.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF01095. Pectinesterase. 1 hit. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit.
PROSITE	PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME52_ARATH

Accession

Primary (citable) accession number: O04953

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	December 14, 2011
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program