PME14_ARATH
ID PME14_ARATH Reviewed; 333 AA.
AC Q9ZQA4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative pectinesterase 14;
DE Short=PE 14;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 14;
DE Short=AtPME14;
DE Flags: Precursor;
GN Name=PME14; Synonyms=ARATH14; OrderedLocusNames=At2g36700;
GN ORFNames=F13K3.10;
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.
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}.
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DR EMBL; AC006282; AAD20146.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09288.1; -; Genomic_DNA.
DR PIR; F84783; F84783.
DR RefSeq; NP_181208.1; NM_129225.1.
DR AlphaFoldDB; Q9ZQA4; -.
DR SMR; Q9ZQA4; -.
DR STRING; 3702.AT2G36700.1; -.
DR PaxDb; Q9ZQA4; -.
DR PRIDE; Q9ZQA4; -.
DR EnsemblPlants; AT2G36700.1; AT2G36700.1; AT2G36700.
DR GeneID; 818242; -.
DR Gramene; AT2G36700.1; AT2G36700.1; AT2G36700.
DR KEGG; ath:AT2G36700; -.
DR Araport; AT2G36700; -.
DR TAIR; locus:2040525; AT2G36700.
DR eggNOG; ENOG502QUTX; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q9ZQA4; -.
DR OMA; NTIGCIT; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9ZQA4; -.
DR BioCyc; ARA:AT2G36700-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9ZQA4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQA4; differential.
DR Genevisible; Q9ZQA4; 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..333
FT /note="Putative pectinesterase 14"
FT /id="PRO_0000371671"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 333 AA; 37067 MW; 5751439F1DF535B7 CRC64;
MLFFILFLSI ISPIESVDQR IHHPSKCDHL SKFPTKGFTM VLKVSLNGCG RFKRVQDAID
ASIGSSQSKT LILIDFGIYR ERFIVHENKN NLVVQGMGYS RTSIEWNNTT ASSNGTFSSF
SVAVFGEKFT AYNISFKNTA PAPNPGAVDA QAVALKVVGD KAAFYGCGFY GNQDTLLDQE
GRHFFKGCFI EGSIDFIFGN GRSLYEDCTL HSIAKENTIG CITANGKDTL KDRTGFVFVN
CKITGSARVW LGRAWRPYAR VIFSKTYMSR VVSLDGWNDM GDPKTQRTVY YGEHRCYGPG
ANHSKRVTYA KLLSDVEAAP FTNISFIDGE EWL
