PME60_ARATH
ID PME60_ARATH Reviewed; 540 AA.
AC Q9FHN4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 60;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 60;
DE AltName: Full=Pectin methylesterase inhibitor 60;
DE Includes:
DE RecName: Full=Pectinesterase 60;
DE Short=PE 60;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 60;
DE Short=AtPME60;
DE Flags: Precursor;
GN Name=PME60; Synonyms=ARATH60; OrderedLocusNames=At5g51500;
GN ORFNames=K17N15.5;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 -!- 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; AB018109; BAB08666.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96091.1; -; Genomic_DNA.
DR RefSeq; NP_199963.1; NM_124529.2.
DR AlphaFoldDB; Q9FHN4; -.
DR SMR; Q9FHN4; -.
DR STRING; 3702.AT5G51500.1; -.
DR iPTMnet; Q9FHN4; -.
DR PaxDb; Q9FHN4; -.
DR PRIDE; Q9FHN4; -.
DR ProteomicsDB; 226271; -.
DR EnsemblPlants; AT5G51500.1; AT5G51500.1; AT5G51500.
DR GeneID; 835224; -.
DR Gramene; AT5G51500.1; AT5G51500.1; AT5G51500.
DR KEGG; ath:AT5G51500; -.
DR Araport; AT5G51500; -.
DR TAIR; locus:2153127; AT5G51500.
DR eggNOG; ENOG502QU67; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9FHN4; -.
DR OMA; ANEALGC; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9FHN4; -.
DR BioCyc; ARA:AT5G51500-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FHN4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHN4; baseline and differential.
DR Genevisible; Q9FHN4; 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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
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 TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..540
FT /note="Probable pectinesterase/pectinesterase inhibitor 60"
FT /id="PRO_0000370179"
FT REGION 32..185
FT /note="Pectinesterase inhibitor 60"
FT REGION 225..526
FT /note="Pectinesterase 60"
FT ACT_SITE 355
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 376
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 302
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 354
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 369..389
FT /evidence="ECO:0000250"
SQ SEQUENCE 540 AA; 59648 MW; B33E471B758CA5D8 CRC64;
MNIMMVQNIS FLSLHLLLIL LLCLRPLTTV ADGNSTNIDG WCDKTPYPYP CKRYFIKHSG
FRLPTQISEF RVLLVEAAMD RAVSAWDKLT NSSKNCTDFK KQAVLADCIN LYGDTVMQLN
RTLQGVSSKT GRRCTDFDAQ TWLSTALTNT ETCRRGSSDL NVSDFTTPIV SNTKISHLIS
NCLAVNGALL TAGKNDSTTG DSKGFPTWVS RKERRLLQLQ SVRANLVVAK DGSGHFKTVQ
AAIDVAGRRK VTSGRFVIYV KRGIYQENLN VRLNNDNIML VGDGMRYTII TGGRSVKGGY
TTYSSATAGI EGLHFIAKGI AFQNTAGPAK GQAVALRSSS DLSIFYRCSI EGYQDTLMVH
SQRQFYRECY IYGTVDFIFG NAAVVFQNCI ILPRLPLKGQ ANVITAQGRT DLFQNTGISI
HNSIIIPAPD LKPVVRSVKT YMGRPWMMYS RTVVLKTYID SVVSPVGWSP WTKGSTYGLD
TLFYAEYKNI GPASSTRWRV RWKGFHVLSK ASDASAFSVG KFIAGTAWLP GSGIPFTSEL
