PME68_ARATH
ID PME68_ARATH Reviewed; 362 AA.
AC Q8LPF3; Q9FGK7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable pectinesterase 68;
DE Short=PE 68;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 68;
DE Short=AtPME68;
DE Flags: Precursor;
GN Name=PME68; Synonyms=ARATH68; OrderedLocusNames=At5g47500; ORFNames=MNJ7.9;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
RP TISSUE SPECIFICITY.
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: Secreted, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025628; BAB09076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95526.1; -; Genomic_DNA.
DR EMBL; AY102117; AAM26686.1; -; mRNA.
DR EMBL; BT000565; AAN18134.1; -; mRNA.
DR RefSeq; NP_199561.1; NM_124123.5.
DR AlphaFoldDB; Q8LPF3; -.
DR SMR; Q8LPF3; -.
DR BioGRID; 20048; 1.
DR STRING; 3702.AT5G47500.1; -.
DR PaxDb; Q8LPF3; -.
DR PRIDE; Q8LPF3; -.
DR ProteomicsDB; 234932; -.
DR EnsemblPlants; AT5G47500.1; AT5G47500.1; AT5G47500.
DR GeneID; 834800; -.
DR Gramene; AT5G47500.1; AT5G47500.1; AT5G47500.
DR KEGG; ath:AT5G47500; -.
DR Araport; AT5G47500; -.
DR TAIR; locus:2169023; AT5G47500.
DR eggNOG; ENOG502QUGG; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q8LPF3; -.
DR OMA; YANEGRQ; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q8LPF3; -.
DR BioCyc; ARA:AT5G47500-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q8LPF3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPF3; baseline and differential.
DR Genevisible; Q8LPF3; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..362
FT /note="Probable pectinesterase 68"
FT /id="PRO_0000371712"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 362 AA; 40042 MW; C1204DCAD999A3B9 CRC64;
MAQLTNSLNY LFSVSLLLFV SFHCLCFRFS LVAACSNSTD DQQIQHHHHR KWVGPSGHKV
ITVSLNGHAQ FRSVQDAVDS IPKNNNKSIT IKIAPGFYRE KVVVPATKPY ITFKGAGRDV
TAIEWHDRAS DLGANGQQLR TYQTASVTVY ANYFTARNIS FTNTAPAPLP GMQGWQAVAF
RISGDKAFFS GCGFYGAQDT LCDDAGRHYF KECYIEGSID FIFGNGRSMY KDCELHSIAS
RFGSIAAHGR TCPEEKTGFA FVGCRVTGTG PLYVGRAMGQ YSRIVYAYTY FDALVAHGGW
DDWDHKSNKS KTAFFGVYNC YGPGAAATRG VSWARALDYE SAHPFIAKSF VNGRHWIAPR
DA
