O81320 (PME38_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative pectinesterase/pectinesterase inhibitor 38

Including the following 2 domains:

1. Pectinesterase inhibitor 38
   Alternative name(s):
   Pectin methylesterase inhibitor 38
2. Pectinesterase 38
   Short name=PE 38
   EC=3.1.1.11
   Alternative name(s):
   Pectin methylesterase 38
   Short name=AtPME38

Gene names

Name:	PME38
Synonyms:	ARATH38
Ordered Locus Names:	At4g00190
ORF Names:	F6N15.23

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	474 AA.
Sequence status	Complete.
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.
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.
Caution	Lacks the conserved signal peptide, which is one of the features of the pectinesterase family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
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
	Chain	1 – 474	474	Putative pectinesterase/pectinesterase inhibitor 38		PRO_0000371688
Regions
	Region	1 – 130	130	Pectinesterase inhibitor 38
	Region	164 – 461	298	Pectinesterase 38
Sites
	Active site	294	1	Proton donor; for pectinesterase activity By similarity
	Active site	315	1	Nucleophile; for pectinesterase activity By similarity
	Binding site	241	1	Substrate; for pectinesterase activity By similarity
	Binding site	271	1	Substrate; for pectinesterase activity By similarity
	Binding site	380	1	Substrate; for pectinesterase activity By similarity
	Binding site	382	1	Substrate; for pectinesterase activity By similarity
	Site	293	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	409	1	N-linked (GlcNAc...) Potential
	Disulfide bond	308 ↔ 328		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O81320 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: B1764AE6DC5FCA9B	FASTA	474	52,417
	10 20 30 40 50 60 MVFGNEMCDE TPHPGECKTL LIKHKPIRST TQFLQVSVER TLDGAVKAKS DTYFLEPQFG 70 80 90 100 110 120 SKQAWEECMD LYEQTIHRLN ESVLCPKNVC SRSDVQAWLS TALTNLDTCQ EEMSELGVSS 130 140 150 160 170 180 HSLESITIDV INTLAINKRM EQNGKEFGIS KITMKTLSIG EKVDVVVAQD GSGDYKTIQE 190 200 210 220 230 240 AVNGAGERLK GSPRYVIHVK QGVYEEYVNV GIKSNNIMIT GDGIGKTIIT GDKSKGRGFS 250 260 270 280 290 300 TYKSATFVAE GDGFVGRDIT IRNTAGPENH QAVALRSNSD MSVFYRCSIE GYQDTLYVHS 310 320 330 340 350 360 GRQFFRECDI YGTVDFIFGN AAAVLQNCRI FARNPPNGVN TITAQSRFNP NQTTGIVIHN 370 380 390 400 410 420 SVVKGAPGVQ LGGVKTYLGR PWRSYARTVV IGTYLDTLIE PNGWIDWDNV TALSTLYYGE 430 440 450 460 470 YQNSGPGSGT ENRVDWAGFH VISDIQEARE FTLPKFIDSA SWLPPTKVPF TINL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [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	AF069299 Genomic DNA. Translation: AAC19295.1. AL161471 Genomic DNA. Translation: CAB80777.1. CP002687 Genomic DNA. Translation: AEE81836.1.
IPI	IPI00525861.
PIR	T01347.
RefSeq	NP_191930.1. NM_116236.1.
UniGene	At.54052.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortal	O81320.
SMR	O81320. Positions 2-143, 159-474.
ModBase	Search...
Proteomic databases
PRIDE	O81320.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G00190.1; AT4G00190.1; AT4G00190.
GeneID	828218.
GenomeReviews	Gene locus AT4G00190 in contig CT486007_GR.
KEGG	ath:AT4G00190.
NMPDR	fig|3702.1.peg.17772.
Organism-specific databases
GeneFarm	306. 8.
TAIR	At4g00190.
Phylogenomic databases
eggNOG	COG4677.
GeneTree	EPGT00070000027901.
HOGENOM	HBG747179.
InParanoid	O81320.
OMA	TIDVINT.
PhylomeDB	O81320.
ProtClustDB	CLSN2916163.
Gene expression databases
ArrayExpress	O81320.
Genevestigator	O81320.
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. False negative. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME38_ARATH

Accession

Primary (citable) accession number: O81320

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	November 1, 1998
Last modified:	December 14, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program