Reviewed, UniProtKB/Swiss-Prot Q9LVQ0 (PME31_ARATH)

Names and origin

Protein names

Recommended name:
    Pectinesterase 31
      Short name=PE 31
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 31
      Short name=AtPME31

Gene names

Name:	PME31
Synonyms:	ARATH31
Ordered Locus Names:	At3g29090
ORF Names:	MXE2.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity. Acts in a blockwise manner, resulting in a cell wall rigidification. Ref.6
Catalytic activity	Pectin + n H2O = n methanol + pectate.
Enzyme regulation	Does not require salt for activity. Not inhibited by kiwi pectin methylesterase inhibitor (PMEI). Ref.6
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Tissue specificity	Expressed in siliques. Ref.5
Developmental stage	Expressed during late developmental phases of siliques. Ref.5
Miscellaneous	This is the only member of the pectinesterase family that do not contain a transmembrane or a signal peptide.
Sequence similarities	Belongs to the pectinesterase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0-8.5. Temperature dependence: Fully active at 0 or 30 degrees Celsius, inactive at 55 degrees Celsius.

Ontologies

Keywords
Molecular function	Aspartyl esterase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro pectin metabolic process Ref.6 Inferred from direct assay. Source: TAIR
Cellular component	cell wall Inferred from electronic annotation. Source: InterPro
Molecular function	aspartyl esterase activity Inferred from electronic annotation. Source: UniProtKB-KW pectinesterase activity Ref.6 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 317	317	Pectinesterase 31		PRO_0000371683
Sites
	Active site	144	1	Proton donor By similarity
	Active site	165	1	Nucleophile By similarity
	Binding site	91	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	222	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity
	Site	143	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LVQ0-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: BCD96098853B585B	FASTA	317	35,520
	10 20 30 40 50 60 MATTRMVRVS QDGSGDYCSV QDAIDSVPLG NTCRTVIRLS PGIYRQPVYV PKRKNFITFA 70 80 90 100 110 120 GISPEITVLT WNNTASKIEH HQASRVIGTG TFGCGSVIVE GEDFIAENIT FENSAPEGSG 130 140 150 160 170 180 QAVAIRVTAD RCAFYNCRFL GWQDTLYLHH GKQYLKDCYI EGSVDFIFGN STALLEHCHI 190 200 210 220 230 240 HCKSQGFITA QSRKSSQEST GYVFLRCVIT GNGQSGYMYL GRPWGPFGRV VLAYTYMDAC 250 260 270 280 290 300 IRNVGWHNWG NAENERSACF YEYRCFGPGS CSSERVPWSR ELMDDEAGHF VHHSFVDPEQ 310 DRPWLCLRMG VKTPYSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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. , 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.
[3]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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.
[5]	"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.
[6]	"Activity of an atypical Arabidopsis thaliana pectin methylesterase." Dedeurwaerder S., Menu-Bouaouiche L., Mareck A., Lerouge P., Guerineau F. Planta 229:311-321(2009) [PubMed: 18936961] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB018121 Genomic DNA. Translation: BAB01985.1. AY070091 mRNA. Translation: AAL49785.1. AY096561 mRNA. Translation: AAM20211.1. AY084418 mRNA. Translation: AAM60992.1.
IPI	IPI00546007.
RefSeq	NP_566842.1.
UniGene	At.28398 Rra.14369
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
SMR	Q9LVQ0. Positions 5-316.
ModBase	Search...
Proteomic databases
PRIDE	Q9LVQ0.
Genome annotation databases
GeneID	822556.
GenomeReviews	Gene locus AT3G29090 in contig BA000014_GR.
KEGG	ath:AT3G29090.
NMPDR	fig|3702.1.peg.15215.
Organism-specific databases
TAIR	At3g29090.
Phylogenomic databases
eggNOG	euNOG09608.
HOGENOM	HBG747179.
InParanoid	Q9LVQ0.
OMA	ENERSAC.
Gene expression databases
ArrayExpress	Q9LVQ0.
Genevestigator	Q9LVQ0.
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]
PROSITE	PS00800. PECTINESTERASE_1. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME31_ARATH

Accession

Primary (citable) accession number: Q9LVQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)