Q96576

SS
Gene name
PME3
Protein name
Pectinesterase 3
Names
PE 3, Pectin methylesterase 3
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)

50-197 (PMEI region) SS

Target domain

233-527 (Pectinesterase domain)

Relief mechanism

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q96576

Entry ID Method Resolution Chain Position Source
AF-Q96576-F1 Predicted AlphaFoldDB

No variants for Q96576

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q96576

No associated diseases with Q96576

4 regional properties for Q96576

Type Name Position InterPro Accession
domain Pectinesterase, catalytic 233 - 527 IPR000070
domain Pectinesterase inhibitor domain 28 - 191 IPR006501
active_site Pectinesterase, Tyr active site 257 - 276 IPR018040
active_site Pectinesterase, Asp active site 375 - 384 IPR033131

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
Q1JPL7 PME18 Pectinesterase/pectinesterase inhibitor 18 Arabidopsis thaliana (Mouse-ear cress) SS
Q1PEC0 PME42 Probable pectinesterase/pectinesterase inhibitor 42 Arabidopsis thaliana (Mouse-ear cress) SS
Q84JX1 PME19 Probable pectinesterase/pectinesterase inhibitor 19 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
Q43143 PMEU1 Pectinesterase/pectinesterase inhibitor U1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q96575 PME2.2 Pectinesterase 2.2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
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