PME58_ARATH
ID PME58_ARATH Reviewed; 571 AA.
AC Q9FJ21;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 58;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 58;
DE AltName: Full=Pectin methylesterase inhibitor 58;
DE Includes:
DE RecName: Full=Pectinesterase 58;
DE Short=PE 58;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 58;
DE Short=AtPME58;
DE Flags: Precursor;
GN Name=PME58; Synonyms=ARATH58; OrderedLocusNames=At5g49180;
GN ORFNames=K21P3.5;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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).
RN [6]
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, but not in flower buds.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expression restricted to early to mid-stage of
CC silique development. Not found in vegetative stage. Expressed in the
CC micropyle area of the ovule just after fertilization.
CC {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; AB016872; BAB10336.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95779.1; -; Genomic_DNA.
DR EMBL; AY075680; AAL77687.1; -; mRNA.
DR EMBL; BT002211; AAN72223.1; -; mRNA.
DR EMBL; AY088442; AAM65978.1; -; mRNA.
DR RefSeq; NP_199729.1; NM_124295.3.
DR AlphaFoldDB; Q9FJ21; -.
DR SMR; Q9FJ21; -.
DR STRING; 3702.AT5G49180.1; -.
DR PaxDb; Q9FJ21; -.
DR PRIDE; Q9FJ21; -.
DR ProteomicsDB; 236574; -.
DR EnsemblPlants; AT5G49180.1; AT5G49180.1; AT5G49180.
DR GeneID; 834977; -.
DR Gramene; AT5G49180.1; AT5G49180.1; AT5G49180.
DR KEGG; ath:AT5G49180; -.
DR Araport; AT5G49180; -.
DR TAIR; locus:2155884; AT5G49180.
DR eggNOG; ENOG502R6WA; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9FJ21; -.
DR OMA; HAHACKK; -.
DR OrthoDB; 714825at2759; -.
DR PhylomeDB; Q9FJ21; -.
DR BioCyc; ARA:AT5G49180-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FJ21; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ21; baseline and differential.
DR Genevisible; Q9FJ21; 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:0048359; P:mucilage metabolic process involved in seed coat development; IMP:TAIR.
DR GO; GO:0048358; P:mucilage pectin biosynthetic process; IMP:TAIR.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..571
FT /note="Probable pectinesterase/pectinesterase inhibitor 58"
FT /id="PRO_0000371706"
FT REGION 49..204
FT /note="Pectinesterase inhibitor 58"
FT REGION 259..556
FT /note="Pectinesterase 58"
FT ACT_SITE 388
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 409
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 335
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 387
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 36
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 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 402..422
FT /evidence="ECO:0000250"
SQ SEQUENCE 571 AA; 62799 MW; 777402570880BBC9 CRC64;
MGVDGELKKK KCIIAGVITA LLVLMVVAVG ITTSRNTSHS EKIVPVQIKT ATTAVEAVCA
PTDYKETCVN SLMKASPDST QPLDLIKLGF NVTIRSIEDS IKKASVELTA KAANDKDTKG
ALELCEKLMN DATDDLKKCL DNFDGFSIPQ IEDFVEDLRV WLSGSIAYQQ TCMDTFEETN
SKLSQDMQKI FKTSRELTSN GLAMITNISN LLGEFNVTGV TGDLGKYARK LLSAEDGIPS
WVGPNTRRLM ATKGGVKANV VVAHDGSGQY KTINEALNAV PKANQKPFVI YIKQGVYNEK
VDVTKKMTHV TFIGDGPTKT KITGSLNYYI GKVKTYLTAT VAINGDNFTA KNIGFENTAG
PEGHQAVALR VSADLAVFYN CQIDGYQDTL YVHSHRQFFR DCTVSGTVDF IFGDGIVVLQ
NCNIVVRKPM KSQSCMITAQ GRSDKRESTG LVLQNCHITG EPAYIPVKSI NKAYLGRPWK
EFSRTIIMGT TIDDVIDPAG WLPWNGDFAL NTLYYAEYEN NGPGSNQAQR VKWPGIKKLS
PKQALRFTPA RFLRGNLWIP PNRVPYMGNF Q
