PME28_ARATH
ID PME28_ARATH Reviewed; 732 AA.
AC Q3E8Z8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative pectinesterase/pectinesterase inhibitor 28;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 28;
DE AltName: Full=Pectin methylesterase inhibitor 28;
DE Includes:
DE RecName: Full=Pectinesterase 28;
DE Short=PE 28;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 28;
DE Short=AtPME28;
GN Name=PME28; Synonyms=ARATH28; OrderedLocusNames=At5g27870;
GN ORFNames=F14I23.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
RA Markovic O., Janecek S.;
RT "Pectin methylesterases: sequence-structural features and phylogenetic
RT relationships.";
RL Carbohydr. Res. 339:2281-2295(2004).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
RA Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
RA Guerineau F., Pelloux J.;
RT "Comprehensive expression profiling of the pectin methylesterase gene
RT family during silique development in Arabidopsis thaliana.";
RL Planta 224:782-791(2006).
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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds.
CC {ECO:0000269|PubMed:16622707}.
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; AC007399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93739.1; -; Genomic_DNA.
DR RefSeq; NP_198139.1; NM_122669.2.
DR AlphaFoldDB; Q3E8Z8; -.
DR SMR; Q3E8Z8; -.
DR STRING; 3702.AT5G27870.1; -.
DR PaxDb; Q3E8Z8; -.
DR PRIDE; Q3E8Z8; -.
DR ProteomicsDB; 236575; -.
DR EnsemblPlants; AT5G27870.1; AT5G27870.1; AT5G27870.
DR GeneID; 832850; -.
DR Gramene; AT5G27870.1; AT5G27870.1; AT5G27870.
DR KEGG; ath:AT5G27870; -.
DR Araport; AT5G27870; -.
DR TAIR; locus:2143340; AT5G27870.
DR eggNOG; ENOG502QPZF; Eukaryota.
DR HOGENOM; CLU_012243_9_0_1; -.
DR InParanoid; Q3E8Z8; -.
DR OMA; ADEAIFY; -.
DR OrthoDB; 714825at2759; -.
DR PhylomeDB; Q3E8Z8; -.
DR BioCyc; ARA:AT5G27870-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q3E8Z8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E8Z8; baseline and differential.
DR Genevisible; Q3E8Z8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
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; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
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.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..732
FT /note="Putative pectinesterase/pectinesterase inhibitor 28"
FT /id="PRO_0000371681"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 51..204
FT /note="Pectinesterase inhibitor 28"
FT REGION 252..548
FT /note="Pectinesterase 28"
FT REGION 570..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 401
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 379
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 394..414
FT /evidence="ECO:0000250"
SQ SEQUENCE 732 AA; 78477 MW; DF433495A0BAAA13 CRC64;
MSYGYDDEDA KRKKRYVIIS ISSVLLISMV VAVTIGVSVN KSDNAGDEEI TTSVKAIKDV
CAPTDYKETC EDTLRKDAKD TSDPLELVKT AFNATMKQIS DVAKKSQTMI ELQKDPRAKM
ALDQCKELMD YAIGELSKSF EELGKFEFHK VDEALVKLRI WLSATISHEQ TCLDGFQGTQ
GNAGETIKKA LKTAVQLTHN GLAMVTEMSN YLGQMQIPEM NSRRLLSQEF PSWMDARARR
LLNAPMSEVK PDIVVAQDGS GQYKTINEAL NFVPKKKNTT FVVHIKEGIY KEYVQVNRSM
THLVFIGDGP DKTVISGSKS YKDGITTYKT ATVAIVGDHF IAKNIAFENT AGAIKHQAVA
IRVLADESIF YNCKFDGYQD TLYAHSHRQF YRDCTISGTI DFLFGDAAAV FQNCTLLVRK
PLLNQACPIT AHGRKDPRES TGFVLQGCTI VGEPDYLAVK EQSKTYLGRP WKEYSRTIIM
NTFIPDFVPP EGWQPWLGEF GLNTLFYSEV QNTGPGAAIT KRVTWPGIKK LSDEEILKFT
PAQYIQGDAW IPGKGVPYIL GLFSGNGSTN STVTGSSLSS NTTESSDSPS TVVTPSTSPP
AGHLGSPSDT PSSVVSPSTS LPAGQLGAPP ATPSMVVSPS TSPPAGHLGS PSDTPSSLVS
PSTSPPAGHL GSPSDTPSSV VTPSASPSTS PSASPSVSPS AFPSASPSAS PSASPSVSPS
ASPSASPQSS IG
