Q96575

SS
Gene name
PME2.2
Protein name
Pectinesterase 2.2
Names
PE 2.2, Pectin methylesterase 2.2
Species
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
KEGG Pathway
EC number
3.1.1.11: Carboxylic ester hydrolases
Protein Class

Descriptions

(Annotation from UniProt)
The PMEI region may act as an autoinhibitory domain.

Autoinhibitory domains (AIDs)

50-201 (PMEI region) SS

Target domain

237-533 (Pectinesterase domain)

Relief mechanism

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q96575

Entry ID Method Resolution Chain Position Source
AF-Q96575-F1 Predicted AlphaFoldDB

No variants for Q96575

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q96575

No associated diseases with Q96575

3 regional properties for Q96575

Type Name Position InterPro Accession
domain Cation-transporting P-type ATPase, N-terminal 13 - 85 IPR004014
ptm P-type ATPase, phosphorylation site 329 - 335 IPR018303
domain P-type ATPase, haloacid dehalogenase domain 309 - 637 IPR044492

Functions

Description
EC Number 3.1.1.11 Carboxylic ester hydrolases
Subcellular Localization
  • Secreted, cell wall
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

3 GO annotations of molecular function

Name Definition
aspartyl esterase activity Catalysis of the hydrolysis of an ester bond by a mechanism involving a catalytically active aspartic acid residue.
pectinesterase activity Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
pectinesterase inhibitor activity Binds to and stops, prevents or reduces the activity of pectinesterase.

3 GO annotations of biological process

Name Definition
cell wall modification The series of events leading to chemical and structural alterations of an existing cell wall that can result in loosening, increased extensibility or disassembly.
fruit ripening An developmental maturation process that has as participant a fruit. Ripening causes changes in one or more characteristics of a fruit (color, aroma, flavor, texture, hardness, cell wall structure) and may make it more attractive to animals and aid in seed dispersal.
pectin catabolic process The chemical reactions and pathways resulting in the breakdown of pectin, a polymer containing a backbone of alpha-1,4-linked D-galacturonic acid residues.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q84JX1 PME19 Probable pectinesterase/pectinesterase inhibitor 19 Arabidopsis thaliana (Mouse-ear cress) SS
Q1PEC0 PME42 Probable pectinesterase/pectinesterase inhibitor 42 Arabidopsis thaliana (Mouse-ear cress) SS
Q1JPL7 PME18 Pectinesterase/pectinesterase inhibitor 18 Arabidopsis thaliana (Mouse-ear cress) SS
P09607 PME2.1 Pectinesterase 2.1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
P14280 PME1.9 Pectinesterase 1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q96576 PME3 Pectinesterase 3 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q43143 PMEU1 Pectinesterase/pectinesterase inhibitor U1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
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
GVAYVDGLYD