PME2_CITSI
ID PME2_CITSI Reviewed; 510 AA.
AC O04887; O04889;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pectinesterase 2;
DE Short=PE 2;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase;
DE Flags: Precursor;
GN Name=PECS-2.1;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Valencia;
RA Nairn C.J., Lewandowski D.J., Burns J.K.;
RT "Genetics and expression of two pectinesterase genes in Valencia orange.";
RL Physiol. Plantarum 102:226-235(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 -!- 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 -!- TISSUE SPECIFICITY: Expressed at low levels in young leaves, young
CC bark, young fruit, mature fruit vesicles, shoots and flower buds, young
CC bark and juice vesicles. In both leaf and fruit abscission zones, and
CC mature leaves, expression was initially undetectable but increased
CC markedly following ethylene treatment. {ECO:0000269|Ref.1}.
CC -!- INDUCTION: By ethylene. {ECO:0000269|Ref.1}.
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; U82975; AAB57669.1; -; Genomic_DNA.
DR EMBL; U82977; AAB57671.1; -; mRNA.
DR PIR; T10491; T10491.
DR PIR; T10494; T10494.
DR RefSeq; NP_001275775.1; NM_001288846.1.
DR AlphaFoldDB; O04887; -.
DR SMR; O04887; -.
DR STRING; 2711.XP_006490884.1; -.
DR GeneID; 102577945; -.
DR KEGG; cit:102577945; -.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR OrthoDB; 674407at2759; -.
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; IPR006633; Carb-bd_sugar_hydrolysis-dom.
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; SM00722; CASH; 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; Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..510
FT /note="Pectinesterase 2"
FT /id="PRO_0000023481"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 349
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 327
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 342..362
FT /evidence="ECO:0000250"
FT CONFLICT 130
FT /note="T -> S (in Ref. 1; AAB57671)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="T -> A (in Ref. 1; AAB57671)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="S -> N (in Ref. 1; AAB57671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 56328 MW; BD4D57D0376A2035 CRC64;
MALRILITVS LVLFSLSHTS FGYSPEEVKS WCGKTPNPQP CEYFLTQKTD VTSIKQDTDF
YKISLQLALE RATTAQSRTY TLGSKCRNER EKAAWEDCRE LYELTVLKLN QTSNSSPGCT
KVDKQTWLST ALTNLETCRA SLEDLGVPEY VLPLLSNNVT KLISNTLSLN KVPYNEPSYK
DGFPTWVKPG DRKLLQTTPR ANIVVAQDGS GNVKTIQEAV AAASRAGGSR YVIYIKAGTY
NENIEVKLKN IMFVGDGIGK TIITGSKSVG GGATTFKSAT VAVVGDNFIA RDITIRNTAG
PNNHQAVALR SGSDLSVFYR CSFEGYQDTL YVHSQRQFYR ECDIYGTVDF IFGNAAVVLQ
NCNIFARKPP NRTNTLTAQG RTDPNQSTGI IIHNCRVTAA SDLKPVQSSV KTFLGRPWKQ
YSRTVYIKTF LDSLINPAGW MEWSGDFALN TLYYAEYMNT GPGSSTANRV KWRGYHVLTS
PSQVSQFTVG NFIAGNSWLP ATNVPFTSGL
