PME29_ARATH
ID PME29_ARATH Reviewed; 335 AA.
AC Q4PSN0; Q9LRN4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable pectinesterase 29;
DE Short=PE 29;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 29;
DE Short=AtPME29;
DE Flags: Precursor;
GN Name=PME29; Synonyms=ARATH29; OrderedLocusNames=At3g24130;
GN ORFNames=MUJ8.16;
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;
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).
RN [5]
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).
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 flower buds.
CC {ECO:0000269|PubMed:16622707}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB028621; BAB01354.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76861.1; -; Genomic_DNA.
DR EMBL; DQ056606; AAY78754.1; -; mRNA.
DR RefSeq; NP_189055.1; NM_113318.2.
DR AlphaFoldDB; Q4PSN0; -.
DR SMR; Q4PSN0; -.
DR STRING; 3702.AT3G24130.1; -.
DR PaxDb; Q4PSN0; -.
DR PRIDE; Q4PSN0; -.
DR ProteomicsDB; 226274; -.
DR EnsemblPlants; AT3G24130.1; AT3G24130.1; AT3G24130.
DR GeneID; 821999; -.
DR Gramene; AT3G24130.1; AT3G24130.1; AT3G24130.
DR KEGG; ath:AT3G24130; -.
DR Araport; AT3G24130; -.
DR TAIR; locus:2093736; AT3G24130.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR HOGENOM; CLU_012243_3_0_1; -.
DR InParanoid; Q4PSN0; -.
DR OMA; AVPINNR; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q4PSN0; -.
DR BioCyc; ARA:AT3G24130-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q4PSN0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q4PSN0; baseline and differential.
DR Genevisible; Q4PSN0; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..335
FT /note="Probable pectinesterase 29"
FT /id="PRO_0000371682"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 187
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 165
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 335 AA; 37272 MW; 1C3CB972B2E66EDB CRC64;
MGTHRIFIGL IALCCFCLPH LIEAKPFGVY QQQVFVDQSG HGNFTTIQKA IDSVPINNRH
WFFINVKAGL YREKIKIPYE KPFIVLVGAG KRLTRVEWDD HYSVAQSPTF STLADNTVVK
SITFANSYNF PSKGKMNKNP RTPAVAALIG GDKSAFYSVG FAGIQDTLWD FDGRHYFHRC
TIQGAVDFIF GTGQSIYQSC VIQVLGGQLE PGLAGYITAQ GRTNPYDANG FIFINCLVYG
TGMAFLGRPW RGYSRVIFYN SNLTDVVVPE GWDAWNFVGH ENQLVFAEHG CFGSGANIGR
RVKWVKKLSE SAIQNLADLS FINRGGWVED LPIPA
