PME10_ARATH
ID PME10_ARATH Reviewed; 339 AA.
AC O64479;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative pectinesterase 10;
DE Short=PE 10;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 10;
DE Short=AtPME10;
DE Flags: Precursor;
GN Name=PME10; Synonyms=ARATH10; OrderedLocusNames=At2g19150;
GN ORFNames=T20K24.17;
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).
RN [4]
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 siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
CC siliques. {ECO:0000269|PubMed:16622707}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; AC002392; AAD12032.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06852.1; -; Genomic_DNA.
DR PIR; T00536; T00536.
DR RefSeq; NP_179505.1; NM_127472.2.
DR AlphaFoldDB; O64479; -.
DR SMR; O64479; -.
DR STRING; 3702.AT2G19150.1; -.
DR PaxDb; O64479; -.
DR PRIDE; O64479; -.
DR EnsemblPlants; AT2G19150.1; AT2G19150.1; AT2G19150.
DR GeneID; 816432; -.
DR Gramene; AT2G19150.1; AT2G19150.1; AT2G19150.
DR KEGG; ath:AT2G19150; -.
DR Araport; AT2G19150; -.
DR TAIR; locus:2059030; AT2G19150.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR HOGENOM; CLU_012243_3_0_1; -.
DR InParanoid; O64479; -.
DR OMA; FKNTHNA; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; O64479; -.
DR BioCyc; ARA:AT2G19150-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:O64479; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64479; baseline and differential.
DR Genevisible; O64479; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..339
FT /note="Putative pectinesterase 10"
FT /id="PRO_0000371667"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
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 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 339 AA; 37633 MW; 5A72930E4D38D912 CRC64;
MKGVTIHNFC YSYFKVCLLV MSLAYGSAEW DGSSSQIAKT IIVNPNDARY FKTVQSAIDS
IPLQNQDWIR ILISNGIYSE KVTIPRGKGY IYMQGGGIEK TIIAYGDHQL TNTSATFTSY
PSNIIITGIT FKNKYNIASS SSPTKPAVAA MMLGDKYAII DSSFDGFQDT LYDDYGRHYY
KRCVISGGID FIFGGAQSIF EGCTLKLRVG IYPPNEVYGT ITAQGRDSPT DKGGFVFKDC
TVMGSGKALL GRAWKSYSRV IFYRSMFSDN ILPIGWDAWK AKGQEGHITF VEFGCTGVGA
DTSKRVPWLT KASEKDVLQF TNLTFIDEEG WLSRLPIKF
