PME_BRACM
ID PME_BRACM Reviewed; 571 AA.
AC Q42608;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Pectinesterase/pectinesterase inhibitor;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor;
DE AltName: Full=Pectin methylesterase inhibitor;
DE Includes:
DE RecName: Full=Pectinesterase;
DE Short=PE;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase;
DE Flags: Fragment;
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Anther;
RA Kim H.U., Park B.S., Lee J.Y., Jin Y.M., Chung T.Y., Kang S.K.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; L48178; AAB04617.1; -; mRNA.
DR PIR; T52325; T52325.
DR AlphaFoldDB; Q42608; -.
DR SMR; Q42608; -.
DR STRING; 3711.Bra007665.1-P; -.
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; Hydrolase;
KW Secreted.
FT CHAIN <1..571
FT /note="Pectinesterase/pectinesterase inhibitor"
FT /id="PRO_0000215044"
FT REGION 27..178
FT /note="Pectinesterase inhibitor"
FT REGION 233..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..558
FT /note="Pectinesterase"
FT ACT_SITE 389
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 410
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 336
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 388
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 571 AA; 61711 MW; 88B56AB6254D87C7 CRC64;
LLVVGVAIGV VTFVNKGGGA GGDKTLNSHQ KAVESLCASA TDKGSCAKTL DPVKSDDPSK
LIKAFMLATK DAVTKSTNFT ASTEEGMGKN MNATSKAVLD YCKRVLMYAL EDLETIVEEM
GEDLQQSGSK MDQLKQWLTG VFNYQTDCID DIEESELRKV MGEGIRHSKI LSSNAIDIFH
ALTTAMSQMN VKVDDMKKGN LGETPAPDRD LLEDLDQKGL PKWHSDKDRK LMAQAGRPGA
PADEGIGEGG GGGGKIKPTH VVAKDGSGQF KTISEAVKAC PEKNPGRCII YIKAGVYKEQ
VTIPKKVNNV FMFGDGATQT IITFDRSVGL SPGTTTSLSG TVQVESEGFM AKWIGFQNTA
GPLGNQAVAF RVNGDRAVIF NCRFDGYQDT LYVNNGRQFY RNIVVSGTVD FINGKSATVI
QNSLILCRKG SPGQTNHVTA DGKQKGKAVK IGIVLHNCRI MADKELEADR LTVKSYLGRP
WKPFATTAVI GTEIGDLIQP TGWNEWQGEK FHLTATYVEF NNRGPGANPA ARVPWAKMAK
SAAEVERFTV ANWLTPANWI QEANVTVQLG L
