PME22_SOLLC
ID PME22_SOLLC Reviewed; 550 AA.
AC Q96575;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pectinesterase 2.2;
DE Short=PE 2.2;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 2.2;
DE Flags: Precursor;
GN Name=PME2.2;
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.;
RT "Fruit-specific pectin methylesterase genomic DNA from Lycopersicon
RT esculentum var. VFNT Cherry.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pectinesterase may play a role in cell wall metabolism during
CC fruit growth and development prior to ripening and may be required for
CC preparing cell walls for softening by polygalacturonase during fruit
CC ripening.
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.
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; U70675; AAB38792.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96575; -.
DR SMR; Q96575; -.
DR PRIDE; Q96575; -.
DR InParanoid; Q96575; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q96575; 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 Disulfide bond; Fruit ripening; Glycoprotein; Hydrolase;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..233
FT /evidence="ECO:0000255"
FT /id="PRO_0000023490"
FT CHAIN 234..550
FT /note="Pectinesterase 2.2"
FT /id="PRO_0000023491"
FT ACT_SITE 365
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 364
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 331..358
FT /evidence="ECO:0000250"
FT DISULFID 399..433
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 60425 MW; BF95179FAD94ED51 CRC64;
MATPQQPLLT KTHKQNSIIS FKILTFVVTL FVALFLVVFL VAPYQFEIKH SNLCKTAQDS
QLCLSYVSDL MSNEIVTTDS DGLSILMKFL VNYVHQMNNA IPVVSKMKNQ INDIRQEGAL
TDCLELLDQS VDLVSDSIAA IDKRTHSEHA NAQSWLSGVL TNHVTCLDEL DSFTKAMING
TNLDELISRA KVALAMLASV TTPNDDVLRP GLGKMPSWVS SRDRKLMESS GKDIGANAVV
AKDGTGKYRT LAEAVAAAPD KSKTRYVIYV KRGIYKENVE VSSRKMKLMI VGDGMHATII
TGNLNVVDGS TTFHSATLAA VGKGFILQDI CIQNTAGPAK HQAVALRVGA DKSVINRCRI
DAYQDTLYAH SQRQFYRDSY VTGTIDFIFG NAAVVFQKCK LVARKPGKYQ QNMVTAQGRT
DPNQATGTSI QFCNIIASSD LEPVLKEFPT YLGRPWKKYS RTVVMESYLG GLINPAGWAE
WDGDFALKTL YYGEFMNNGP GAGTSKRVKW PGYHCITDPA EAMPFTVAKL IQGGSWLRST
GVAYVDGLYD
