Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

272-568 (Pectinesterase domain)

Relief mechanism

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q43143

Entry ID Method Resolution Chain Position Source
AF-Q43143-F1 Predicted AlphaFoldDB

No variants for Q43143

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q43143

No associated diseases with Q43143

4 regional properties for Q43143

Type Name Position InterPro Accession
domain Pectinesterase, catalytic 272 - 568 IPR000070
domain Pectinesterase inhibitor domain 59 - 224 IPR006501
active_site Pectinesterase, Tyr active site 297 - 316 IPR018040
active_site Pectinesterase, Asp active site 416 - 425 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.

2 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.
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.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q42534 PME2 Pectinesterase 2 Arabidopsis thaliana (Mouse-ear cress) SS
O49006 PME3 Pectinesterase/pectinesterase inhibitor 3 Arabidopsis thaliana (Mouse-ear cress) SS
P14280 PME1.9 Pectinesterase 1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
P09607 PME2.1 Pectinesterase 2.1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q96576 PME3 Pectinesterase 3 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q96575 PME2.2 Pectinesterase 2.2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
10 20 30 40 50 60
MTRVEDFFSK QIDFCKRKKK IYLAIVASVL LVAAVIGVVA GVKSHSKNSD DHADIMAISS
70 80 90 100 110 120
SAHAIVKSAC SNTLHPELCY SAIVNVSDFS KKVTSQKDVI ELSLNITVKA VRRNYYAVKE
130 140 150 160 170 180
LIKTRKGLTP REKVALHDCL ETMDETLDEL HTAVEDLELY PNKKSLKEHV EDLKTLISSA
190 200 210 220 230 240
ITNQETCLDG FSHDEADKKV RKVLLKGQKH VEKMCSNALA MICNMTDTDI ANEMKLSAPA
250 260 270 280 290 300
NNRKLVEDNG EWPEWLSAGD RRLLQSSTVT PDVVVAADGS GDYKTVSEAV RKAPEKSSKR
310 320 330 340 350 360
YVIRIKAGVY RENVDVPKKK TNIMFMGDGK SNTIITASRN VQDGSTTFHS ATVVRVAGKV
370 380 390 400 410 420
LARDITFQNT AGASKHQAVA LCVGSDLSAF YRCDMLAYQD TLYVHSNRQF FVQCLVAGTV
430 440 450 460 470 480
DFIFGNGAAV FQDCDIHARR PGSGQKNMVT AQGRTDPNQN TGIVIQKCRI GATSDLRPVQ
490 500 510 520 530 540
KSFPTYLGRP WKEYSRTVIM QSSITDVIQP AGWHEWNGNF ALDTLFYGEY ANTGAGAPTS
550 560 570 580
GRVKWKGHKV ITSSTEAQAY TPGRFIAGGS WLSSTGFPFS LGL