PME63_ARATH
ID PME63_ARATH Reviewed; 338 AA.
AC Q9FKF3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative pectinesterase 63;
DE Short=PE 63;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 63;
DE Short=AtPME63;
DE Flags: Precursor;
GN Name=PME63; Synonyms=ARATH63; OrderedLocusNames=At5g61680;
GN ORFNames=K11J9.6;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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: Secreted, cell wall {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012239; BAB09012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001318857.1; NM_001345486.1.
DR AlphaFoldDB; Q9FKF3; -.
DR SMR; Q9FKF3; -.
DR STRING; 3702.AT5G61680.1; -.
DR PaxDb; Q9FKF3; -.
DR PeptideAtlas; Q9FKF3; -.
DR GeneID; 836290; -.
DR KEGG; ath:AT5G61680; -.
DR Araport; AT5G61680; -.
DR TAIR; locus:2151586; AT5G61680.
DR eggNOG; ENOG502R3C8; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q9FKF3; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9FKF3; -.
DR BioCyc; ARA:AT5G61680-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FKF3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKF3; baseline and differential.
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 3: Inferred from homology;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..338
FT /note="Putative pectinesterase 63"
FT /id="PRO_0000371708"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 37324 MW; 430DBDBBF559526A CRC64;
MGYNYVSLIV TILLVVITSP VVFGNDAAPI PENKGRIEQW FNTNVKQNGR GHFKTITEAI
NSVRAGNTRR VIIKIGPGVY KEKVTIDRSK PFITLYGHPN AMPVLTFDGT AAQYGTVDSA
TLIVLSDYFM AVNIILKNSA PMPDGKRKGA QALSMRISGN KAAFYNCKFY GYQDTICDDT
GNHFFKDCYI EGTFDFIFGS GRSLYLGTQL NVVGDGIRVI TAHAGKSAAE KSGYSFVHCK
VTGTGTGIYL GRSWMSHPKV VYAYTDMSSV VNPSGWQENR EAGRDKTVFY GEYKCTGTGS
HKEKRVKYTQ DIDDIEAKYF ISLGYIQGSS WLLPPPSF
