PME66_ARATH
ID PME66_ARATH Reviewed; 336 AA.
AC Q4PSQ5; O22902;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable pectinesterase 66;
DE Short=PE 66;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 66;
DE Short=AtPME66;
DE Flags: Precursor;
GN Name=PME66; Synonyms=ARATH66; OrderedLocusNames=At2g47280;
GN ORFNames=T8I13.12;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-336.
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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).
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 -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002337; AAB63828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10823.1; -; Genomic_DNA.
DR EMBL; DQ056581; AAY78730.1; -; mRNA.
DR PIR; C84913; C84913.
DR RefSeq; NP_850471.2; NM_180140.2.
DR AlphaFoldDB; Q4PSQ5; -.
DR SMR; Q4PSQ5; -.
DR STRING; 3702.AT2G47280.1; -.
DR PaxDb; Q4PSQ5; -.
DR PRIDE; Q4PSQ5; -.
DR EnsemblPlants; AT2G47280.1; AT2G47280.1; AT2G47280.
DR GeneID; 819341; -.
DR Gramene; AT2G47280.1; AT2G47280.1; AT2G47280.
DR KEGG; ath:AT2G47280; -.
DR Araport; AT2G47280; -.
DR TAIR; locus:2065145; AT2G47280.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q4PSQ5; -.
DR OMA; YAENSCR; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q4PSQ5; -.
DR BioCyc; ARA:AT2G47280-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q4PSQ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q4PSQ5; baseline and differential.
DR Genevisible; Q4PSQ5; 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; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..336
FT /note="Probable pectinesterase 66"
FT /id="PRO_0000371710"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 163
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 336 AA; 37017 MW; 5041C5F58A49939C CRC64;
MKRVASYNYK IVCMVVMTLF VYGYSAAAEQ IAYTITVDLN GGGNFTTVQS AIDSISPPNH
NWIRVFTQNG IYREKVTIPK EKGFIYLQGK GIEQTVIEYD DHQATDISAT FTAFADDIVI
SGITFKNTYN IVPNNKREIV PAVAARMLGD RYVVTDSSFV GLQDTLFDGK GRHYYKRCII
SGGIDFIFGY GQSLFKECTL NMTLGIYAPD NPYGTITAHQ RPSPSDEGGF VFSDCTVTGV
GKTLLGRAWG SNARVIFDRS RLSDVVLPIG WDAWRAKGNE RDLTFVEAGC TGAGADTSQR
VPWLKKLSLS EVDGFASVSF IDQDGWISRF PIEGGP
