PME11_ARATH
ID PME11_ARATH Reviewed; 352 AA.
AC Q9SIJ9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative pectinesterase 11;
DE Short=PE 11;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 11;
DE Short=AtPME11;
GN Name=PME11; Synonyms=ARATH11; OrderedLocusNames=At2g21610;
GN ORFNames=F2G1.12;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
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 -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; AC007119; AAD23644.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07202.1; -; Genomic_DNA.
DR PIR; C84603; C84603.
DR RefSeq; NP_179755.1; NM_127732.2.
DR AlphaFoldDB; Q9SIJ9; -.
DR SMR; Q9SIJ9; -.
DR STRING; 3702.AT2G21610.1; -.
DR PaxDb; Q9SIJ9; -.
DR EnsemblPlants; AT2G21610.1; AT2G21610.1; AT2G21610.
DR GeneID; 816699; -.
DR Gramene; AT2G21610.1; AT2G21610.1; AT2G21610.
DR KEGG; ath:AT2G21610; -.
DR Araport; AT2G21610; -.
DR TAIR; locus:2049344; AT2G21610.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_012243_3_0_1; -.
DR InParanoid; Q9SIJ9; -.
DR PhylomeDB; Q9SIJ9; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9SIJ9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIJ9; baseline and differential.
DR Genevisible; Q9SIJ9; 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: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; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase; Glycoprotein; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Putative pectinesterase 11"
FT /id="PRO_0000371668"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 332..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 196
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 39058 MW; B166A3E21A4A525D CRC64;
MGLYKTKSKR SIANYHHIII INIFILSSIT SSSMASSSSP SSIDFSTAIL IRVDQSGKGD
FSKIQEAIES IPPNLNNSQL YFIWVKPGIY REKVVIPAEK PYITLSGTQA SNTFLIWSDG
EDILESPTLT IFASDFVCRF LTIQNKFGTA GRAVALRVAA DKAAFYGCVI TSYQDTLLDD
NGNHYFKNCY IEGATDFICG SASSLYERCH LHSLSPNNGS ITAQMRTSAT EKSGFTFLGC
KLTGSGSTFL GRPWGAYSRV VFAYSFFSNV VAPQGWNQWG DSTKENTVYY GEYKCYGPGA
DREQRVEWSK QLSDEEATVF LSKDFIGGKD WLRPAPSHFK NAPKQTQNKE IN
