Q96576 (PME3_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectinesterase 3
Short name=PE 3
EC=3.1.1.11

Alternative name(s):
Pectin methylesterase 3

Gene names

Name:

PME3

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	544 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 Probable.
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 Fruit ripening
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Aspartyl esterase Hydrolase
PTM	Glycoprotein Zymogen
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 ripening 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 – ?		Potential
	Chain	? – 544		Pectinesterase 3		PRO_0000023492
Sites
	Active site	359	1	Proton donor By similarity
	Active site	380	1	Nucleophile By similarity
	Binding site	306	1	Substrate By similarity
	Binding site	336	1	Substrate By similarity
	Binding site	448	1	Substrate By similarity
	Binding site	450	1	Substrate By similarity
	Site	358	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	174	1	N-linked (GlcNAc...) Potential
	Glycosylation	257	1	N-linked (GlcNAc...) Potential
	Glycosylation	291	1	N-linked (GlcNAc...) Potential
	Glycosylation	532	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q96576 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 35793B47D74EFDA7	FASTA	544	60,249
	10 20 30 40 50 60 MATPLQPFLT KTHKQNPIIG FNILTFVVTL FVALFLVVFL VAPYQFEIKH SNLCKTAQDS 70 80 90 100 110 120 QLCLSYVSEI VTTESDGVTV LKKFLVKYVH QMNNAIPVVR KIKNQINDIR QQGALTDCLE 130 140 150 160 170 180 LLDQSVDLVS DSIAAIDKRS RSEHANAQSW LSGVLTNHVT CLDELTSFSL STKNGTVLDE 190 200 210 220 230 240 LITRAKVALA MLASVTTPND EVLRQGLGKM PYWVSSRDRK LMESSGKDII ANRVVAQDGT 250 260 270 280 290 300 GDYQTLAEAV AAAPDKNKTR YVIYVKMGIY KENVVVTKKK MNLMIVGDGM NATIITGSLN 310 320 330 340 350 360 VVDGSTFPSN TLAAVGQGFI LQDICIQNTA GPEKDQAVAL RVGADMSVIN RCRIDAYQDT 370 380 390 400 410 420 LYAHSQRQFY RDSYVTGTVD FIFGNAAVVF QKCQIVARKP NKRQKNMVTA QGRTDPNQAT 430 440 450 460 470 480 GTSIQFCDII ASPDLEPVMN EYKTYLGRPW KKHSRTVVMQ SYLDGHIDPS GWFEWRGDFA 490 500 510 520 530 540 LKTLYYGEFM NNGPGAGTSK RVKWPGYHVI TDPNEAMPFT VAELIQGGSW LNSTSVAYVE GLVE

References

[1]	Turner L.A., Harriman R.W., Handa A.K. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. VFNT Cherry.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U70676 Genomic DNA. Translation: AAB38793.1.
PIR	T07593.
3D structure databases
ProteinModelPortal	Q96576.
SMR	Q96576. Positions 229-544.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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

PME3_SOLLC

Accession

Primary (citable) accession number: Q96576

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	May 31, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program