PME16_ARATH
ID PME16_ARATH Reviewed; 518 AA.
AC Q9SKX2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 16;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 16;
DE AltName: Full=Pectin methylesterase inhibitor 16;
DE Includes:
DE RecName: Full=Pectinesterase 16;
DE Short=PE 16;
DE EC=3.1.1.11;
DE AltName: Full=AtPMEpcrD;
DE AltName: Full=Pectin methylesterase 16;
DE Short=AtPME16;
DE Flags: Precursor;
GN Name=PME16; Synonyms=ARATH16; OrderedLocusNames=At2g43050; ORFNames=MFL8.9;
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA Micheli F., Holliger C., Goldberg R., Richard L.;
RT "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT member of a gene family comprising at least 12 genes in Arabidopsis
RT thaliana.";
RL Gene 220:13-20(1998).
RN [5]
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 -!- TISSUE SPECIFICITY: Expressed in siliques and floral stems.
CC {ECO:0000269|PubMed:9767082}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
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DR EMBL; AC006224; AAD22126.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10203.1; -; Genomic_DNA.
DR EMBL; BT023433; AAY56424.1; -; mRNA.
DR PIR; D84861; D84861.
DR RefSeq; NP_181833.1; NM_129866.5.
DR AlphaFoldDB; Q9SKX2; -.
DR SMR; Q9SKX2; -.
DR STRING; 3702.AT2G43050.1; -.
DR PaxDb; Q9SKX2; -.
DR PRIDE; Q9SKX2; -.
DR ProteomicsDB; 235046; -.
DR EnsemblPlants; AT2G43050.1; AT2G43050.1; AT2G43050.
DR GeneID; 818907; -.
DR Gramene; AT2G43050.1; AT2G43050.1; AT2G43050.
DR KEGG; ath:AT2G43050; -.
DR Araport; AT2G43050; -.
DR TAIR; locus:2053728; AT2G43050.
DR eggNOG; ENOG502QRAG; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9SKX2; -.
DR OMA; THKSIGE; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9SKX2; -.
DR BioCyc; ARA:AT2G43050-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9SKX2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKX2; baseline and differential.
DR Genevisible; Q9SKX2; 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:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
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 InterPro; IPR006501; Pectinesterase_inhib_dom.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..518
FT /note="Probable pectinesterase/pectinesterase inhibitor 16"
FT /id="PRO_0000371673"
FT REGION 30..172
FT /note="Pectinesterase inhibitor 16"
FT REGION 213..502
FT /note="Pectinesterase 16"
FT ACT_SITE 342
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 363
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 289
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 341
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 56589 MW; C5E7A903F0786604 CRC64;
MASSSSISNH KIPNTLMFLV IVNFLYLIQT NSAVSISSNS NSHFSRFSRH RSSPSSKTKQ
GFLATVQESM NHALLARSLA FNLTLSHRTV QTHTFDPIHD CLELLDDTLD MLSRIHADND
EEDVHTWLSA ALTNQDTCEQ SLQEKSESYK HGLAMDFVAR NLTGLLTSSL DLFVSVKSKH
RKLLSKQEYF PTFVPSSEQR RLLEAPVEEL NVDAVVAPDG SGTHKTIGEA LLSTSLASSG
GRTKIYLKAG TYHENINIPT KQKNVMLVGD GKGKTVIVGS RSNRGGWTTY KTATVAAMGE
GFIARDMTFV NNAGPKSEQA VALRVGADKS VVHRCSVEGY QDSLYTHSKR QFYRETDITG
TVDFIFGNSA VVFQSCNIAA RKPLPGQRNF VTAQGRSNPG QNTGIAIQNC RITAESMTYL
GRPWKEYSRT VVMQSFIGGS IHPSGWSPWS GGFGLKSLFY GEYGNSGPGS SVSGRVKWSG
CHPSLTVTEA EKFTVASFID GNIWLPSTGV SFDPGLVN
