PME31_ARATH
ID PME31_ARATH Reviewed; 317 AA.
AC Q9LVQ0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Pectinesterase 31;
DE Short=PE 31;
DE EC=3.1.1.11 {ECO:0000269|PubMed:18936961};
DE AltName: Full=Pectin methylesterase 31;
DE Short=AtPME31;
GN Name=PME31; Synonyms=ARATH31; OrderedLocusNames=At3g29090; ORFNames=MXE2.5;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND 3D-STRUCTURE MODELING.
RX PubMed=18936961; DOI=10.1007/s00425-008-0831-0;
RA Dedeurwaerder S., Menu-Bouaouiche L., Mareck A., Lerouge P., Guerineau F.;
RT "Activity of an atypical Arabidopsis thaliana pectin methylesterase.";
RL Planta 229:311-321(2009).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin (PubMed:18936961). Acts in a
CC blockwise manner, resulting in a cell wall rigidification.
CC {ECO:0000250, ECO:0000269|PubMed:18936961}.
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 Evidence={ECO:0000269|PubMed:18936961};
CC -!- ACTIVITY REGULATION: Does not require salt for activity. Not inhibited
CC by kiwi pectin methylesterase inhibitor (PMEI).
CC {ECO:0000269|PubMed:18936961}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:18936961};
CC Temperature dependence:
CC Fully active at 0 or 30 degrees Celsius, inactive at 55 degrees
CC Celsius. {ECO:0000269|PubMed:18936961};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- INTERACTION:
CC Q9LVQ0; Q93ZX1: RFC4; NbExp=4; IntAct=EBI-4466887, EBI-4470690;
CC -!- TISSUE SPECIFICITY: Expressed in siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
CC siliques. {ECO:0000269|PubMed:16622707}.
CC -!- MISCELLANEOUS: This is the only member of the pectinesterase family
CC that do not contain a transmembrane or a signal peptide.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; AB018121; BAB01985.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77534.1; -; Genomic_DNA.
DR EMBL; AY070091; AAL49785.1; -; mRNA.
DR EMBL; AY096561; AAM20211.1; -; mRNA.
DR EMBL; AY084418; AAM60992.1; -; mRNA.
DR RefSeq; NP_566842.1; NM_113832.4.
DR AlphaFoldDB; Q9LVQ0; -.
DR SMR; Q9LVQ0; -.
DR BioGRID; 7885; 3.
DR IntAct; Q9LVQ0; 2.
DR STRING; 3702.AT3G29090.1; -.
DR PaxDb; Q9LVQ0; -.
DR PRIDE; Q9LVQ0; -.
DR ProteomicsDB; 236645; -.
DR EnsemblPlants; AT3G29090.1; AT3G29090.1; AT3G29090.
DR GeneID; 822556; -.
DR Gramene; AT3G29090.1; AT3G29090.1; AT3G29090.
DR KEGG; ath:AT3G29090; -.
DR Araport; AT3G29090; -.
DR TAIR; locus:2094652; AT3G29090.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR HOGENOM; CLU_012243_3_1_1; -.
DR InParanoid; Q9LVQ0; -.
DR OMA; NRVAWCR; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9LVQ0; -.
DR BioCyc; ARA:AT3G29090-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9LVQ0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVQ0; baseline and differential.
DR Genevisible; Q9LVQ0; AT.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0030599; F:pectinesterase activity; IDA:TAIR.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
DR GO; GO:0045488; P:pectin metabolic process; IDA:TAIR.
DR Gene3D; 2.160.20.10; -; 1.
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 Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Aspartyl esterase; Hydrolase; Reference proteome.
FT CHAIN 1..317
FT /note="Pectinesterase 31"
FT /id="PRO_0000371683"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 35520 MW; BCD96098853B585B CRC64;
MATTRMVRVS QDGSGDYCSV QDAIDSVPLG NTCRTVIRLS PGIYRQPVYV PKRKNFITFA
GISPEITVLT WNNTASKIEH HQASRVIGTG TFGCGSVIVE GEDFIAENIT FENSAPEGSG
QAVAIRVTAD RCAFYNCRFL GWQDTLYLHH GKQYLKDCYI EGSVDFIFGN STALLEHCHI
HCKSQGFITA QSRKSSQEST GYVFLRCVIT GNGQSGYMYL GRPWGPFGRV VLAYTYMDAC
IRNVGWHNWG NAENERSACF YEYRCFGPGS CSSERVPWSR ELMDDEAGHF VHHSFVDPEQ
DRPWLCLRMG VKTPYSA
