PME47_ARATH
ID PME47_ARATH Reviewed; 624 AA.
AC Q9FF77;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 47;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 47;
DE AltName: Full=Pectin methylesterase inhibitor 47;
DE Includes:
DE RecName: Full=Pectinesterase 47;
DE Short=PE 47;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 47;
DE Short=AtPME47;
DE Flags: Precursor;
GN Name=PME47; Synonyms=ARATH47; OrderedLocusNames=At5g04970;
GN ORFNames=MUG13.17;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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).
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 -!- 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; AB005245; BAB11519.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90810.1; -; Genomic_DNA.
DR RefSeq; NP_196116.1; NM_120579.3.
DR AlphaFoldDB; Q9FF77; -.
DR SMR; Q9FF77; -.
DR STRING; 3702.AT5G04970.1; -.
DR PaxDb; Q9FF77; -.
DR PRIDE; Q9FF77; -.
DR ProteomicsDB; 234881; -.
DR EnsemblPlants; AT5G04970.1; AT5G04970.1; AT5G04970.
DR GeneID; 830379; -.
DR Gramene; AT5G04970.1; AT5G04970.1; AT5G04970.
DR KEGG; ath:AT5G04970; -.
DR Araport; AT5G04970; -.
DR TAIR; locus:2175334; AT5G04970.
DR eggNOG; ENOG502QT2B; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9FF77; -.
DR OMA; FVIYARA; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9FF77; -.
DR BioCyc; ARA:AT5G04970-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FF77; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF77; baseline and differential.
DR Genevisible; Q9FF77; 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 Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..624
FT /note="Probable pectinesterase/pectinesterase inhibitor 47"
FT /id="PRO_0000371695"
FT REGION 24..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..236
FT /note="Pectinesterase inhibitor 47"
FT REGION 307..606
FT /note="Pectinesterase 47"
FT COMPBIAS 25..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 459
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 385
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 527
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 437
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 452..472
FT /evidence="ECO:0000250"
SQ SEQUENCE 624 AA; 68148 MW; 80D388C903AC5E9A CRC64;
MQTHSSSLVF LALLCLSWAL LVSPTRPPSQ PPSHPPIQPS SQPPTQPPSQ PPTQPPTQPP
SHPPTQPPTP PPSQSPSQPS PLPPNIACKS TPYPKLCRTI LSAVKSSPSD PYHYGKFTMK
QCLKQARRLS KVINRFAQRV EADPGTSTVE EVSAVADCGE LAELSVEYLE TVTEELKAAE
LMTAALVDRV TSLLGGVVTN QQTCLDGLVD AKSGFATAIG TPLGNLTRLY SVSLGLVSHA
LNRNLKRYKG SKGKIFGGGN KPVREPLETL IKVLRKTCDK GKDCRKANRN LGELGETSGG
SILVREAVTV GPYETDNFPT ITEAVAAAPN HTFPEQGYFV IYARAGLYEE YVVISNKKRN
IMLIGDGINK TIISGNHSFI DGWTTYNSST FAVVGDRFVA VDVTFRNTAG PEKHQAVAVR
NNADGSTFYR CSFEGYQDTL YVHSLRQFYR ECDIYGTIDF IFGNAAAIFQ NCNIYARKPM
ANQKNAVTAH GRTDPNQKTG ISIINCTIGA APDLAADPKS TMTFLGRPWK PYSRTVYIQS
YISDVVQPVG WLEWNGTTGL DTISYGEYDN FGPGADTSKR VQWSGYSLLN LVQAMNFTVY
NFTLGDTWLP QTDIPFYGGL LHTE
