PME59_ARATH
ID PME59_ARATH Reviewed; 536 AA.
AC Q9FHN5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 59;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 59;
DE AltName: Full=Pectin methylesterase inhibitor 59;
DE Includes:
DE RecName: Full=Pectinesterase 59;
DE Short=PE 59;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 59;
DE Short=AtPME59;
DE Flags: Precursor;
GN Name=PME59; Synonyms=ARATH59; OrderedLocusNames=At5g51490;
GN ORFNames=K17N15.4;
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; BAB08665.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96090.1; -; Genomic_DNA.
DR RefSeq; NP_199962.1; NM_124528.3.
DR AlphaFoldDB; Q9FHN5; -.
DR SMR; Q9FHN5; -.
DR STRING; 3702.AT5G51490.1; -.
DR PaxDb; Q9FHN5; -.
DR PRIDE; Q9FHN5; -.
DR ProteomicsDB; 235047; -.
DR EnsemblPlants; AT5G51490.1; AT5G51490.1; AT5G51490.
DR GeneID; 835223; -.
DR Gramene; AT5G51490.1; AT5G51490.1; AT5G51490.
DR KEGG; ath:AT5G51490; -.
DR Araport; AT5G51490; -.
DR TAIR; locus:2153112; AT5G51490.
DR eggNOG; ENOG502QU67; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9FHN5; -.
DR OMA; GLFVIYV; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9FHN5; -.
DR BioCyc; ARA:AT5G51490-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FHN5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHN5; baseline and differential.
DR Genevisible; Q9FHN5; 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..536
FT /note="Probable pectinesterase/pectinesterase inhibitor 59"
FT /id="PRO_0000370180"
FT REGION 31..183
FT /note="Pectinesterase inhibitor 59"
FT REGION 221..522
FT /note="Pectinesterase 59"
FT ACT_SITE 351
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 372
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 298
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 350
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
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 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
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 365..385
FT /evidence="ECO:0000250"
SQ SEQUENCE 536 AA; 58868 MW; 17FBC0F027F35BF9 CRC64;
MNMMMQKLSI LFLHLILLVL LCVHPLTTVA DRNSTDWCDK TPYPDPCKCY FKNHNGFQQP
TQLSEFRVML VEAAMDRAIS ARAELTNSGK NCTDSKKQAV LADCIDLYGD TIMQLNRTLH
GVSPKAGAAK SCTDFDAQTW LSTALTNTET CRRGSSDLNV TDFITPIVSN TKISHLISNC
LAVNGALLTA GNKGNTTANQ KGFPTWLSRK DKRLLRAVRA NLVVAKDGSG HFNTVQAAID
VAGRRKVTSG RFVIYVKRGI YQENINVRLN NDDIMLVGDG MRSTIITGGR SVQGGYTTYN
SATAGIEGLH FIAKGITFRN TAGPAKGQAV ALRSSSDLSI FYKCSIEGYQ DTLMVHSQRQ
FYRECYIYGT VDFIFGNAAA VFQNCLILPR RPLKGQANVI TAQGRADPFQ NTGISIHNSR
ILPAPDLKPV VGTVKTYMGR PWMKFSRTVV LQTYLDNVVS PVGWSPWIEG SVFGLDTLFY
AEYKNTGPAS STRWRVSWKG FHVLGRASDA SAFTVGKFIA GTAWLPRTGI PFTSGL
