Reviewed, UniProtKB/Swiss-Prot Q9LXD9 (PME51_ARATH)

Names and origin

Protein names

Recommended name:
    Probable pectinesterase/pectinesterase inhibitor 51
Including the following 2 domains:
    1- Recommended name:
            Pectinesterase inhibitor 51
        Alternative name(s):
            Pectin methylesterase inhibitor 51
    2- Recommended name:
            Pectinesterase 51
                Short name=PE 51
              EC=3.1.1.11
        Alternative name(s):
            Pectin methylesterase 51
              Short name=AtPME51

Gene names

Name:	PME51
Synonyms:	ARATH51
Ordered Locus Names:	At5g09760
ORF Names:	F17I14.50

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	551 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 throughout silique development. Ref.4
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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro
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 enzyme inhibitor activity Inferred from electronic annotation. Source: InterPro 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 – 20	20	Potential
	Chain	21 – 551	531	Probable pectinesterase/pectinesterase inhibitor 51		PRO_0000371699
Regions
	Region	39 – 189	151	Pectinesterase inhibitor 51
	Region	240 – 544	305	Pectinesterase 51
	Compositional bias	23 – 27	5	Poly-His
Sites
	Active site	370	1	Proton donor; for pectinesterase activity By similarity
	Active site	391	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	317	1	Substrate; for pectinesterase activity By similarity
	Binding site	347	1	Substrate; for pectinesterase activity By similarity
	Binding site	467	1	Substrate; for pectinesterase activity By similarity
	Binding site	469	1	Substrate; for pectinesterase activity By similarity
	Site	369	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	108	1	N-linked (GlcNAc...) Potential
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Disulfide bond	384 ↔ 404		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LXD9-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0367BA2E4E1CE789	FASTA	551	60,439
	10 20 30 40 50 60 MSSILILLFS LFLFSSPSSS SRHHHHHNSG DTSPVNPSSS LAAQIRLACN ATRYPDQCVS 70 80 90 100 110 120 SLSEQGRVPP DPKPIQIIHS AISFSFQNLK TAQSKIKSIV DSSVGNLNRT NAANTCLQLL 130 140 150 160 170 180 TYSEHRTQST DQALTRGKIK DARAWMSAAL VYQYDSWSAL KYVNDTSQVG ETMSFLDGLI 190 200 210 220 230 240 HVTSNALSMM VSYDNFGDNV ASWTYPATER DGFWEKTGPG LGLDPSTGLN LGFPSGLKED 250 260 270 280 290 300 VTVCKDGKCG YKTVQDAVNA APEDNGMRKF VIKISEGVYE ENVIVPFEKK NVVFIGDGMG 310 320 330 340 350 360 KTVITGSLNA GMPGITTYNT ATVGVVGDGF MARDLTFQNT AGPDAHQAVA FRSDSDFSLI 370 380 390 400 410 420 ENCEFLGNQD TLYAHGLRQF YKNCRIQGNV DFIFGNSAAV FQDCEILIAP RQINPEKGEK 430 440 450 460 470 480 NAVTAQGRID PSQSTGFVFL NCLINGTEEY MKLFKANPKV HKNFLGRPWK DYSRTVFIGC 490 500 510 520 530 540 NLEALITPDG WLPWSGDFAL KTLYYGESKN TGPGSDRSQR VSWSSQIPDE HVHVYSVANF 550 IQADEWASMS A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S. DNA Res. 6:183-195(1999) [PubMed: 10470850] [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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB020752 Genomic DNA. Translation: BAB09534.1. Different initiation. AL353994 Genomic DNA. Translation: CAB89354.1. AY070093 mRNA. Translation: AAL49830.1. BT006059 mRNA. Translation: AAP04044.1.
IPI	IPI00536110.
PIR	T49922.
RefSeq	NP_196538.1.
UniGene	At.28396
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBase	Search...
Proteomic databases
PRIDE	Q9LXD9.
Genome annotation databases
GeneID	830836.
GenomeReviews	Gene locus AT5G09760 in contig BA000015_GR.
KEGG	ath:AT5G09760.
NMPDR	fig|3702.1.peg.23100.
Organism-specific databases
TAIR	At5g09760.
Phylogenomic databases
OMA	RTISDAM.
Gene expression databases
ArrayExpress	Q9LXD9.
Genevestigator	Q9LXD9.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR018040. Pectinesterase_AS. IPR000070. Pectinesterase_cat. IPR006501. Pectinesterase_inhib. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit. G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.
Pfam	PF01095. Pectinesterase. 1 hit. PF04043. PMEI. 1 hit. [Graphical view]
TIGRFAMs	TIGR01614. PME_inhib. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. False negative. PS00503. PECTINESTERASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME51_ARATH

Accession

Primary (citable) accession number: Q9LXD9
Secondary accession number(s): Q9FXW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)