PME_BRANA
ID PME_BRANA Reviewed; 584 AA.
AC P41510;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable 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: Precursor;
GN Name=BP19;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Westar; TISSUE=Pollen;
RX PubMed=1868195; DOI=10.1007/bf00023417;
RA Albani D., Altosaar I., Arnison P.G., Fabijanski S.F.;
RT "A gene showing sequence similarity to pectin esterase is specifically
RT expressed in developing pollen of Brassica napus. Sequences in its 5'
RT flanking region are conserved in other pollen-specific promoters.";
RL Plant Mol. Biol. 16:501-513(1991).
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: Pollen, and at much lower levels in pistils and
CC petals.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during microspore 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}.
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DR EMBL; X56195; CAA39658.1; -; Genomic_DNA.
DR PIR; S14952; S14952.
DR AlphaFoldDB; P41510; -.
DR SMR; P41510; -.
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 Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..584
FT /note="Probable pectinesterase/pectinesterase inhibitor"
FT /id="PRO_0000023479"
FT REGION 40..191
FT /note="Pectinesterase inhibitor"
FT REGION 246..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..571
FT /note="Pectinesterase"
FT ACT_SITE 402
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 423
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 349
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 401
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 584 AA; 62939 MW; 643887AA7F3AE6CE CRC64;
MAVGKIVISV ASMLLVVGVA IGVVTFVNKG GGAGGDKTLN SHQKAVESLC ASATDKGSCA
KTLDPVKSDD PSKLIKAFML ATKDAVTKST NFTASTEEGM GKNINATSKA VLDYCKRVLM
YALEDLETIV EEMGEDLQQS GSKMDQLKQW LTGVFNYQTD CIDDIEESEL RKVMGEGIAH
SKILSSNAID IFHALTTAMS QMNVKVDDMK KGNLGETPAP DRDLLEDLDQ KGLPKWHSDK
DRKLMAQAGR PGAPADEGIG EGGGGGGKIK PTHVVAKDGS GQFKTISEAV KACPEKNPGR
CIIYIKAGVY KEQVTIPKKV NNVFMFGDGA TQTIITFDRS VGLSPGTTTS LSGTVQVESE
GFMAKWIGFQ NTAGPLGHQA VAFRVNGDRA VIFNCRFDGY QDTLYVNNGR QFYRNIVVSG
TVDFIFGKSA TVIQNSLILC RKGSPGQTNH VTADGNEKGK AVKIGIVLHN CRIMADKELE
ADRLTVKSYL GRPWKPFATT AVIGTEIGDL IQPTGWNEWQ GEKFHLTATY VEFNNRGPGA
NTAARVPWAK MAKSAAEVER FTVANWLTPA NWIQEANVPV QLGL
