PME21_SOLLC
ID PME21_SOLLC Reviewed; 550 AA.
AC P09607; Q43144; Q43777;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Pectinesterase 2.1;
DE Short=PE 2.1;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 2.1;
DE Flags: Precursor;
GN Name=PME2.1;
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 [MRNA].
RC STRAIN=cv. Ailsa Craig; TISSUE=Pericarp;
RX PubMed=8018878; DOI=10.1007/bf00023246;
RA Hall L.N., Bird C.R., Picton S., Tucker G.A., Seymour G.B., Grierson D.;
RT "Molecular characterisation of cDNA clones representing pectin esterase
RT isozymes from tomato.";
RL Plant Mol. Biol. 25:313-318(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rutgers; TISSUE=Fruit;
RA Turner L.A., Kausch K.D., Handa A.K.;
RT "Isolation and nucleotide sequence of two cDNAs corresponding to tomato
RT fruit pectin methylesterase genes.";
RL (er) Plant Gene Register PGR96-035(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-550.
RX PubMed=3371355; DOI=10.1111/j.1432-1033.1988.tb14070.x;
RA Ray J., Knapp J., Grierson D., Bird C., Schuch W.;
RT "Identification and sequence determination of a cDNA clone for tomato
RT pectin esterase.";
RL Eur. J. Biochem. 174:119-124(1988).
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 -!- DEVELOPMENTAL STAGE: In ripening fruit.
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; X74639; CAA52704.1; -; mRNA.
DR EMBL; U50985; AAB67739.1; -; mRNA.
DR EMBL; X07910; CAA30746.1; -; mRNA.
DR EMBL; A15983; CAA01257.1; -; Unassigned_RNA.
DR PIR; S46528; S46528.
DR RefSeq; NP_001233948.1; NM_001247019.1.
DR AlphaFoldDB; P09607; -.
DR SMR; P09607; -.
DR STRING; 4081.Solyc07g064180.2.1; -.
DR PaxDb; P09607; -.
DR GeneID; 544289; -.
DR KEGG; sly:544289; -.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR InParanoid; P09607; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; P09607; -.
DR BRENDA; 3.1.1.11; 3101.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P09607; 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 2: Evidence at transcript level;
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_0000023488"
FT CHAIN 234..550
FT /note="Pectinesterase 2.1"
FT /id="PRO_0000023489"
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"
FT CONFLICT 377..378
FT /note="RD -> QS (in Ref. 3; CAA30746/CAA01257)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="Y -> S (in Ref. 3; CAA30746/CAA01257)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="V -> C (in Ref. 2; AAB67739)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="D -> DYSDIKLLFVYVTRHL (in Ref. 3; CAA30746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 60500 MW; 7ABB7CC37E849DE7 CRC64;
MATPQQPLLT KTHKQNSIIS FKILTFVVTL FVALFLVVFL VAPYQFEIKH SNLCKTAQDS
QLCLSYVSDL ISNEIVTSDS DGLSILKKFL VYSVHQMNNA IPVVRKIKNQ INDIREQGAL
TDCLELLDLS VDLVCDSIAA IDKRSRSEHA NAQSWLSGVL TNHVTCLDEL DSFTKAMING
TNLDELISRA KVALAMLASV TTPNDEVLRP GLGKMPSWVS SRDRKLMESS GKDIGANAVV
AKDGTGKYRT LAEAVAAAPD KSKTRYVIYV KRGTYKENVE VSSRKMNLMI IGDGMYATII
TGSLNVVDGS TTFHSATLAA VGKGFILQDI CIQNTAGPAK HQAVALRVGA DKSVINRCRI
DAYQDTLYAH SQRQFYRDSY VTGTIDFIFG NAAVVFQKCQ LVARKPGKYQ QNMVTAQGRT
DPNQATGTSI QFCDIIASPD LKPVVKEFPT YLGRPWKKYS RTVVMESYLG GLIDPSGWAE
WHGDFALKTL YYGEFMNNGP GAGTSKRVKW PGYHVITDPA EAMSFTVAKL IQGGSWLRST
DVAYVDGLYD
