PME46_ARATH
ID PME46_ARATH Reviewed; 564 AA.
AC Q9FF78; Q84W31;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 46;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 46;
DE AltName: Full=Pectin methylesterase inhibitor 46;
DE Includes:
DE RecName: Full=Pectinesterase 46;
DE Short=PE 46;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 46;
DE Short=AtPME46;
GN Name=PME46; Synonyms=ARATH46; OrderedLocusNames=At5g04960;
GN ORFNames=MUG13.18;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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; BAB11518.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90809.1; -; Genomic_DNA.
DR EMBL; BT004297; AAO42295.1; -; mRNA.
DR EMBL; BT020587; AAW80860.1; -; mRNA.
DR RefSeq; NP_196115.1; NM_120578.5.
DR AlphaFoldDB; Q9FF78; -.
DR SMR; Q9FF78; -.
DR STRING; 3702.AT5G04960.1; -.
DR PaxDb; Q9FF78; -.
DR PRIDE; Q9FF78; -.
DR ProteomicsDB; 234880; -.
DR EnsemblPlants; AT5G04960.1; AT5G04960.1; AT5G04960.
DR GeneID; 830378; -.
DR Gramene; AT5G04960.1; AT5G04960.1; AT5G04960.
DR KEGG; ath:AT5G04960; -.
DR Araport; AT5G04960; -.
DR TAIR; locus:2175319; AT5G04960.
DR eggNOG; ENOG502QVDS; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9FF78; -.
DR OMA; YSEFQNF; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9FF78; -.
DR BioCyc; ARA:AT5G04960-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FF78; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF78; baseline and differential.
DR Genevisible; Q9FF78; AT.
DR GO; GO:0016021; C:integral component of membrane; 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; IMP:TAIR.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1902066; P:regulation of cell wall pectin metabolic process; IMP:TAIR.
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 TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..564
FT /note="Probable pectinesterase/pectinesterase inhibitor 46"
FT /id="PRO_0000370188"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 62..207
FT /note="Pectinesterase inhibitor 46"
FT REGION 257..550
FT /note="Pectinesterase 46"
FT ACT_SITE 385
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 406
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 332
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 384
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 399..419
FT /evidence="ECO:0000250"
FT CONFLICT 464
FT /note="I -> T (in Ref. 3; AAO42295)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="G -> D (in Ref. 3; AAO42295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 62170 MW; 0D3318722F2C0B99 CRC64;
MSSYGRLDEH EQAKLEASRK TKKRIAIIAI SSIVLVCIVV GAVVGTTARD NSKKPPTENN
GEPISVSVKA LCDVTLHKEK CFETLGSAPN ASRSSPEELF KYAVKVTITE LSKVLDGFSN
GEHMDNATSA AMGACVELIG LAVDQLNETM TSSLKNFDDL RTWLSSVGTY QETCMDALVE
ANKPSLTTFG ENHLKNSTEM TSNALAIITW LGKIADTVKF RRRRLLETGN AKVVVADLPM
MEGRRLLESG DLKKKATIVV AKDGSGKYRT IGEALAEVEE KNEKPTIIYV KKGVYLENVR
VEKTKWNVVM VGDGQSKTIV SAGLNFIDGT PTFETATFAV FGKGFMARDM GFINTAGPAK
HQAVALMVSA DLSVFYKCTM DAFQDTMYAH AQRQFYRDCV ILGTVDFIFG NAAVVFQKCE
ILPRRPMKGQ QNTITAQGRK DPNQNTGISI HNCTIKPLDN LTDIQTFLGR PWKDFSTTVI
MKSFMDKFIN PKGWLPWTGD TAPDTIFYAE YLNSGPGAST KNRVKWQGLK TSLTKKEANK
FTVKPFIDGN NWLPATKVPF NSDF
