Q9M9W7 (PME22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative pectinesterase/pectinesterase inhibitor 22

Including the following 2 domains:

1. Pectinesterase inhibitor 22
   Alternative name(s):
   Pectin methylesterase inhibitor 22
2. Pectinesterase 22
   Short name=PE 22
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 22
   Short name=AtPME22

Gene names

Name:	PME22
Synonyms:	ARATH22
Ordered Locus Names:	At3g05620
ORF Names:	F18C1.11

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	543 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.
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 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 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 – 19	19	Potential
	Chain	20 – 543	524	Putative pectinesterase/pectinesterase inhibitor 22		PRO_0000371678
Regions
	Region	38 – 197	160	Pectinesterase inhibitor 22
	Region	240 – 527	288	Pectinesterase 22
	Compositional bias	131 – 134	4	Poly-Gly
	Compositional bias	144 – 147	4	Poly-Ala
	Compositional bias	285 – 288	4	Poly-Lys
Sites
	Active site	368	1	Proton donor; for pectinesterase activity By similarity
	Active site	389	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	315	1	Substrate; for pectinesterase activity By similarity
	Binding site	345	1	Substrate; for pectinesterase activity By similarity
	Binding site	448	1	Substrate; for pectinesterase activity By similarity
	Binding site	450	1	Substrate; for pectinesterase activity By similarity
	Site	367	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
	Glycosylation	263	1	N-linked (GlcNAc...) Potential
	Disulfide bond	382 ↔ 402		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9M9W7 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 012165468B4C084F	FASTA	543	60,806
	10 20 30 40 50 60 MGITTALLLV MLMSVHTSSY ETTILKPYKE DNFRSLVAKA CQFIDAHELC VSNIWTHVKE 70 80 90 100 110 120 SGHGLNPHSV LRAAVKEAHD KAKLAMERIP TVMMLSIRSR EQVAIEDCKE LVGFSVTELA 130 140 150 160 170 180 WSMLEMNKLH GGGGIDLDDG SHDAAAAGGN LKTWLSAAMS NQDTCLEGFE GTERKYEELI 190 200 210 220 230 240 KGSLRQVTQL VSNVLDMYTQ LNALPFKASR NESVIASPEW LTETDESLMM RHDPSVMHPN 250 260 270 280 290 300 TVVAIDGKGK YRTINEAINE APNHSTKRYV IYVKKGVYKE NIDLKKKKTN IMLVGDGIGQ 310 320 330 340 350 360 TIITGDRNFM QGLTTFRTAT VAVSGRGFIA KDITFRNTAG PQNRQAVALR VDSDQSAFYR 370 380 390 400 410 420 CSVEGYQDTL YAHSLRQFYR DCEIYGTIDF IFGNGAAVLQ NCKIYTRVPL PLQKVTITAQ 430 440 450 460 470 480 GRKSPNQNTG FVIQNSYVLA TQPTYLGRPW KLYSRTVYMN TYMSQLVQPR GWLEWFGNFA 490 500 510 520 530 540 LDTLWYGEYN NIGPGWRSSG RVKWPGYHIM DKRTALSFTV GSFIDGRRWL PATGVTFTAG LAN

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC011620 Genomic DNA. Translation: AAF26135.1. CP002686 Genomic DNA. Translation: AEE74267.1.
IPI	IPI00526672.
RefSeq	NP_187213.1. NM_111435.1.
UniGene	At.53193.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	Q9M9W7.
SMR	Q9M9W7. Positions 237-542.
ModBase	Search...
Proteomic databases
PRIDE	Q9M9W7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G05620.1; AT3G05620.1; AT3G05620.
GeneID	819728.
GenomeReviews	Gene locus AT3G05620 in contig BA000014_GR.
KEGG	ath:AT3G05620.
NMPDR	fig|3702.1.peg.12547.
Organism-specific databases
GeneFarm	334. 8.
TAIR	At3g05620.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000027901.
HOGENOM	HBG747179.
InParanoid	Q9M9W7.
OMA	QDTCLEG.
PhylomeDB	Q9M9W7.
ProtClustDB	PLN02506.
Gene expression databases
Genevestigator	Q9M9W7.
Family and domain databases
InterPro	IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. 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]
SMART	SM00856. PMEI. 1 hit. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit. SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMs	TIGR01614. PME_inhib. 1 hit.
PROSITE	PS00800. PECTINESTERASE_1. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME22_ARATH

Accession

Primary (citable) accession number: Q9M9W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program