PME3_SOLLC
ID PME3_SOLLC Reviewed; 544 AA.
AC Q96576;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pectinesterase 3;
DE Short=PE 3;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 3;
DE Flags: Precursor;
GN Name=PME3;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. VFNT Cherry;
RA Turner L.A., Harriman R.W., Handa A.K.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
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}.
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DR EMBL; U70676; AAB38793.1; -; Genomic_DNA.
DR PIR; T07593; T07593.
DR AlphaFoldDB; Q96576; -.
DR SMR; Q96576; -.
DR STRING; 4081.Solyc07g064190.1.1; -.
DR PaxDb; Q96576; -.
DR PRIDE; Q96576; -.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR InParanoid; Q96576; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q96576; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Fruit ripening; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..544
FT /note="Pectinesterase 3"
FT /id="PRO_0000023492"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 358
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 544 AA; 60249 MW; 35793B47D74EFDA7 CRC64;
MATPLQPFLT KTHKQNPIIG FNILTFVVTL FVALFLVVFL VAPYQFEIKH SNLCKTAQDS
QLCLSYVSEI VTTESDGVTV LKKFLVKYVH QMNNAIPVVR KIKNQINDIR QQGALTDCLE
LLDQSVDLVS DSIAAIDKRS RSEHANAQSW LSGVLTNHVT CLDELTSFSL STKNGTVLDE
LITRAKVALA MLASVTTPND EVLRQGLGKM PYWVSSRDRK LMESSGKDII ANRVVAQDGT
GDYQTLAEAV AAAPDKNKTR YVIYVKMGIY KENVVVTKKK MNLMIVGDGM NATIITGSLN
VVDGSTFPSN TLAAVGQGFI LQDICIQNTA GPEKDQAVAL RVGADMSVIN RCRIDAYQDT
LYAHSQRQFY RDSYVTGTVD FIFGNAAVVF QKCQIVARKP NKRQKNMVTA QGRTDPNQAT
GTSIQFCDII ASPDLEPVMN EYKTYLGRPW KKHSRTVVMQ SYLDGHIDPS GWFEWRGDFA
LKTLYYGEFM NNGPGAGTSK RVKWPGYHVI TDPNEAMPFT VAELIQGGSW LNSTSVAYVE
GLVE
