Q3E989 (PME54_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable pectinesterase/pectinesterase inhibitor 54

Including the following 2 domains:

1. Pectinesterase inhibitor 54
   Alternative name(s):
   Pectin methylesterase inhibitor 54
2. Pectinesterase 54
   Short name=PE 54
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 54
   Short name=AtPME54

Gene names

Name:	PME54
Synonyms:	ARATH54
Ordered Locus Names:	At5g20860
ORF Names:	F22D1.30

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	512 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
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 – 24	24	Potential
	Chain	25 – 512	488	Probable pectinesterase/pectinesterase inhibitor 54		PRO_0000371702
Regions
	Region	29 – 193	165	Pectinesterase inhibitor 54
	Region	229 – 496	268	Pectinesterase 54
Sites
	Active site	325	1	Proton donor; for pectinesterase activity By similarity
	Active site	346	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	302	1	Substrate; for pectinesterase activity By similarity
	Binding site	415	1	Substrate; for pectinesterase activity By similarity
	Binding site	417	1	Substrate; for pectinesterase activity By similarity
	Site	324	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	131	1	N-linked (GlcNAc...) Potential
	Disulfide bond	339 ↔ 359		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3E989 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: C0A5DDE69CCE2BFE	FASTA	512	56,699
	10 20 30 40 50 60 MGVIDMVLFW VLLVNALLIV DASSRNMPFA YQNEMQRHCS STKYTSLCVQ NLREFRHGSL 70 80 90 100 110 120 DGLDFVSFLV NKTISDSNLL IPPLSSSMGS SKLVSLEDST YTLPSPSVSD SCERLMKMST 130 140 150 160 170 180 RRLRQAMEAL NGSSRKRHTK HDVQTWLSAA MTFQQACKDS ILDSGGSSSA SAISHISQKM 190 200 210 220 230 240 DHLSRLVSNS LTLVDTIMKN PKPKTKSTAL PRWVTAGERR LLVGRARAHV VVAKDGSGDY 250 260 270 280 290 300 RTVMEAVTAA HGNGKDLTVI VGDDSATGGT SVPDTATMTV TGDGFIARDI GIKNIAGPRG 310 320 330 340 350 360 HQAIALSITS DQSVLYRCSI SGYQDTLYAA ALRQFYRECD IYGTIDFIFG NAAAVFQSCN 370 380 390 400 410 420 IFLRRPHGVK AYNVILANGR TDQRQNTGFA LHSCRIRTDS DLSPVKHKYS SYLGRPWRKY 430 440 450 460 470 480 SRAIVMESYI DDAIAEGGWA GWLDSGDEVL KTLYFGEFKN YGPKARISKR VTWEGFHSIG 490 500 510 FEEANYFSVV KRRNGEDVTN GFKYKFKIKI QI

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	AF296834 Genomic DNA. No translation available. CP002688 Genomic DNA. Translation: AED92898.1.
IPI	IPI00537895.
RefSeq	NP_197586.1. NM_122093.1.
UniGene	At.54935.
3D structure databases
ProteinModelPortal	Q3E989.
SMR	Q3E989. Positions 226-511.
ModBase	Search...
Proteomic databases
PRIDE	Q3E989.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G20860.1; AT5G20860.1; AT5G20860.
GeneID	832209.
GenomeReviews	Gene locus AT5G20860 in contig BA000015_GR.
KEGG	ath:AT5G20860.
NMPDR	fig|3702.1.peg.24299.
Organism-specific databases
TAIR	At5g20860.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000027901.
HOGENOM	HBG747179.
InParanoid	Q3E989.
OMA	DSCERLM.
PhylomeDB	Q3E989.
ProtClustDB	PLN02698.
Gene expression databases
Genevestigator	Q3E989.
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	PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME54_ARATH

Accession

Primary (citable) accession number: Q3E989

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	November 8, 2005
Last modified:	December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program