Reviewed, UniProtKB/Swiss-Prot Q96575 (PME22_SOLLC)

Names and origin

Protein names

Recommended name:
    Pectinesterase 2.2
      Short name=PE 2.2
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase 2.2

Gene names

Name:

PME2.2

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	550 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	Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening.
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.
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	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	cell wall modification Inferred from electronic annotation. Source: InterPro 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
	Propeptide	? – 233		Potential		PRO_0000023490
	Chain	234 – 550	317	Pectinesterase 2.2		PRO_0000023491
Sites
	Active site	365	1	Proton donor By similarity
	Active site	386	1	Nucleophile By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	342	1	Substrate By similarity
	Binding site	454	1	Substrate By similarity
	Binding site	456	1	Substrate By similarity
	Site	364	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Disulfide bond	331 ↔ 358		By similarity
	Disulfide bond	399 ↔ 433		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96575-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: BF95179FAD94ED51	FASTA	550	60,425
	10 20 30 40 50 60 MATPQQPLLT KTHKQNSIIS FKILTFVVTL FVALFLVVFL VAPYQFEIKH SNLCKTAQDS 70 80 90 100 110 120 QLCLSYVSDL MSNEIVTTDS DGLSILMKFL VNYVHQMNNA IPVVSKMKNQ INDIRQEGAL 130 140 150 160 170 180 TDCLELLDQS VDLVSDSIAA IDKRTHSEHA NAQSWLSGVL TNHVTCLDEL DSFTKAMING 190 200 210 220 230 240 TNLDELISRA KVALAMLASV TTPNDDVLRP GLGKMPSWVS SRDRKLMESS GKDIGANAVV 250 260 270 280 290 300 AKDGTGKYRT LAEAVAAAPD KSKTRYVIYV KRGIYKENVE VSSRKMKLMI VGDGMHATII 310 320 330 340 350 360 TGNLNVVDGS TTFHSATLAA VGKGFILQDI CIQNTAGPAK HQAVALRVGA DKSVINRCRI 370 380 390 400 410 420 DAYQDTLYAH SQRQFYRDSY VTGTIDFIFG NAAVVFQKCK LVARKPGKYQ QNMVTAQGRT 430 440 450 460 470 480 DPNQATGTSI QFCNIIASSD LEPVLKEFPT YLGRPWKKYS RTVVMESYLG GLINPAGWAE 490 500 510 520 530 540 WDGDFALKTL YYGEFMNNGP GAGTSKRVKW PGYHCITDPA EAMPFTVAKL IQGGSWLRST 550 GVAYVDGLYD

References

[1]	"Fruit-specific pectin methylesterase genomic DNA from Lycopersicon esculentum var. VFNT Cherry." Turner L.A., Harriman R.W., Handa A.K. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. VFNT Cherry.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U70675 Genomic DNA. Translation: AAB38792.1.
3D structure databases
HSSP	HSSP built from PDB template 1GQ8 based on UniProtKB P83218.
SMR	Q96575. Positions 234-550.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.11. 281054.
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. 1 hit. PS00503. PECTINESTERASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PME22_SOLLC

Accession

Primary (citable) accession number: Q96575

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	September 22, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)