PME3_CITSI
ID PME3_CITSI Reviewed; 584 AA.
AC P83948;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Pectinesterase 3;
DE Short=PE 3;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 3;
DE Flags: Precursor;
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 267-279; 302-305; 308-320;
RP 323-330; 351-364; 393-404; 448-466; 469-506 AND 548-579, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Peelings;
RX PubMed=9821684; DOI=10.1007/s004250050426;
RA Christensen T.M.I.E., Nielsen J.E., Kreiberg J.D., Rasmussen P.,
RA Mikkelsen J.D.;
RT "Pectin methyl esterase from orange fruit: characterization and
RT localization by in-situ hybridization and immunohistochemistry.";
RL Planta 206:493-503(1998).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC Evidence={ECO:0000269|PubMed:9821684};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9821684}.
CC -!- TISSUE SPECIFICITY: In the peel, expression is localized to the region
CC of the flavedo close to the oil glands, and to the innermost layer of
CC the albedo. In the lamella, expression is localized to the cell layers
CC opposing the fruit tissue, and to the parenchyma surrounding the
CC vascular tissue. In the fruit vesicles, expression is restricted to the
CC peripheral cell layers and stalk cells. High levels of expression are
CC detected in the core matrix. {ECO:0000269|PubMed:9821684}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P83948; -.
DR SMR; P83948; -.
DR STRING; 2711.XP_006465802.1; -.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR BRENDA; 3.1.1.11; 1426.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Secreted; Signal.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT PROPEP 51..266
FT /evidence="ECO:0000255"
FT /id="PRO_0000023482"
FT CHAIN 267..584
FT /note="Pectinesterase 3"
FT /id="PRO_0000023483"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 400
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 415..435
FT /evidence="ECO:0000250"
SQ SEQUENCE 584 AA; 63574 MW; E4C17683195311F6 CRC64;
MTRIKEFFTK LSESSTNQNI SNIPKKKKKL FLALFATLLV VAAVIGIVAG VNSRKNSGDN
GNEPHHAILK SSCSSTRYPD LCFSAIAAVP EASKKVTSQK DVIEMSLNIT TTAVEHNYFG
IQKLLKRTNL TKREKVALHD CLETIDETLD ELHKAVEDLE EYPNKKSLSQ HADDLKTLMS
AAMTNQGTCL DGFSHDDANK HVRDALSDGQ VHVEKMCSNA LAMIKNMTDT DMMIMRTSNN
RKLIEETSTV DGWPAWLSTG DRRLLQSSSV TPNVVVAADG SGNFKTVAAS VAAAPQGGTK
RYIIRIKAGV YRENVEVTKK HKNIMFIGDG RTRTIITGSR NVVDGSTTFK SATVAVVGEG
FLARDITFQN TAGPSKHQAV ALRVGADLSA FYNCDMLAYQ DTLYVHSNRQ FFVNCLIAGT
VDFIFGNAAA VLQNCDIHAR KPNSGQKNMV TAQGRADPNQ NTGIVIQKSR IGATSDLKPV
QGSFPTYLGR PWKEYSRTVI MQSSITDVIH PAGWHEWDGN FALNTLFYGE HQNAGAGAGT
SGRVKWKGFR VITSATEAQA FTPGSFIAGS SWLGSTGFPF SLGL
