PME_PRUPE
ID PME_PRUPE Reviewed; 522 AA.
AC Q43062;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor PPE8B;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor PPE8B;
DE AltName: Full=Pectin methylesterase inhibitor PPE8B;
DE Includes:
DE RecName: Full=Pectinesterase PPE8B;
DE Short=PE PPE8B;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase PPE8B;
DE Flags: Precursor;
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Coronet; TISSUE=Fruit;
RA Glover H., Brady C.J., Lee E., Speirs J.;
RT "Multiple pectin esterase genes are expressed in ripening peach fruit:
RT nucleotide sequence of a cDNA encoding peach pectin esterase.";
RL (er) Plant Gene Register PGR96-094(1996).
CC -!- FUNCTION: May have roles in the deposition of pectin in developing
CC tissues and in the wall loosening and cell separation that occurs in
CC cell expansion, fruit ripening and abscission.
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 -!- DEVELOPMENTAL STAGE: Present throughout fruit development.
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X95991; CAA65237.1; -; mRNA.
DR AlphaFoldDB; Q43062; -.
DR SMR; Q43062; -.
DR STRING; 3760.EMJ05525; -.
DR PRIDE; Q43062; -.
DR eggNOG; ENOG502QRGV; Eukaryota.
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 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..522
FT /note="Pectinesterase/pectinesterase inhibitor PPE8B"
FT /id="PRO_0000023497"
FT REGION 31..174
FT /note="Pectinesterase inhibitor PPE8B"
FT REGION 208..506
FT /note="Pectinesterase PPE8B"
FT ACT_SITE 336
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 357
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 283
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 335
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 350..370
FT /evidence="ECO:0000250"
SQ SEQUENCE 522 AA; 57397 MW; 6F9211A516C7949A CRC64;
MPYLLMASHN PLPAGKQLLL LVLLCAFFSS SFIPFASCSI TDDLQTQCLK VSATEFAGSL
KDTIDAVQQV ASILSQFANA FGDFRLANAI SDCLDLLDFS ADELNWSLSA SQNQKGKNNS
TGKLSSDLRT WLSAALVNQD TCSNGFEGTN SIVQGLISAG LGQVTSLVQE LLTQVHPNSN
QQGPNGQIPS WVKTKDRKLL QADGVSVDAI VAQDGTGNFT NVTDAVLAAP DYSMRRYVIY
IKRGTYKENV EIKKKKWNLM MIGDGMDATI ISGNRSFVDG WTTFRSATFA VSGRGFIARD
ITFENTAGPE KHQAVALRSD SDLSVFYRCN IRGYQDTLYT HTMRQFYRDC KISGTVDFIF
GDATVVFQNC QILAKKGLPN QKNSITAQGR KDPNEPTGIS IQFCNITADS DLEAASVNST
PTYLGRPWKL YSRTVIMQSF LSNVIRPEGW LEWNGDFALN SLFYGEYMNY GPGAGLGSRV
KWPGYQVFNE STQAKNYTVA QFIEGNLWLP STGVKYTAEF GV
