PME1_CITSI
ID PME1_CITSI Reviewed; 584 AA.
AC O04886; O04888;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Pectinesterase 1;
DE Short=PE 1;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase;
DE Flags: Precursor;
GN Name=PECS-1.1;
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 high levels in flower buds, shoots and
CC young leaves, and at lower levels in young fruit, young bark and juice
CC vesicles. Not expressed at significant levels in leaf abscission zones
CC following ethylene treatment or in mature leaves. In fruit abscission
CC zones, expression was initially undetectable but increased markedly
CC 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; U82973; AAB57667.1; -; Genomic_DNA.
DR EMBL; U82976; AAB57670.1; -; mRNA.
DR PIR; T10485; T10485.
DR RefSeq; NP_001275859.1; NM_001288930.1.
DR AlphaFoldDB; O04886; -.
DR SMR; O04886; -.
DR PRIDE; O04886; -.
DR GeneID; 102578056; -.
DR KEGG; cit:102578056; -.
DR OrthoDB; 674407at2759; -.
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 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..584
FT /note="Pectinesterase 1"
FT /id="PRO_0000023480"
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"
FT CONFLICT 354
FT /note="A -> V (in Ref. 1; AAB57670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 63513 MW; A6E516A295092202 CRC64;
MTHIKEFFTK LSESSSNQNI SNIPKKKKKL FLALFATLLV VAAVIGIVAG VNSRKNSGDN
GNEPHHAILK SSCSSTRYPD LCFSAIAAVP EASKKVTSQK DVIEMSLNIT TTAVEHNYFG
IQKLLKRTNL TKREKVALHD CLETIDETLD ELHKAVEDLE EYPNKKSLSQ HADDLKTLMS
AAMTNQGTCL DGFSHDDANK HVRDALSDGQ VHVEKMCSNA LAMIKNMTDT DMMIMRTSNN
RKLTEETSTV DGWPAWLSPG DRRLLQSSSV TPNAVVAADG SGNFKTVAAA VAAAPQGGTK
RYIIRIKAGV YRENVEVTKK HKNIMFIGDG RTRTIITGSR NVVDGSTTFK SATAAVVGEG
FLARDITFQN TAGPSKHQAV ALRVGADLSA FYNCDMLAYQ DTLYVHSNRQ FFVNCLIAGT
VDFIFGNAAA VLQNCDIHAR KPNSGQKNMV TAQGRTDPNQ NTGIVIQKSR IGATSDLKPV
QGSFPTYLGR PWKEYSRTVI MQSSITDLIH PAGWHEWDGN FALNTLFYGE HQNSGAGAGT
SGRVKWKGFR VITSATEAQA FTPGSFIAGS SWLGSTGFPF SLGL
