PME57_ARATH
ID PME57_ARATH Reviewed; 246 AA.
AC Q9MAL0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative pectinesterase 57;
DE Short=PE 57;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 57;
DE Short=AtPME57;
GN Name=PME57; Synonyms=ARATH57; OrderedLocusNames=At1g44980;
GN ORFNames=F27F5.7;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
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 -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF69174.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007915; AAF69174.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32070.1; -; Genomic_DNA.
DR PIR; H96508; H96508.
DR RefSeq; NP_175118.2; NM_103578.2.
DR AlphaFoldDB; Q9MAL0; -.
DR SMR; Q9MAL0; -.
DR BioGRID; 26288; 1.
DR STRING; 3702.AT1G44980.1; -.
DR PaxDb; Q9MAL0; -.
DR PRIDE; Q9MAL0; -.
DR EnsemblPlants; AT1G44980.1; AT1G44980.1; AT1G44980.
DR GeneID; 841063; -.
DR Gramene; AT1G44980.1; AT1G44980.1; AT1G44980.
DR KEGG; ath:AT1G44980; -.
DR Araport; AT1G44980; -.
DR TAIR; locus:2028250; AT1G44980.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_1130412_0_0_1; -.
DR InParanoid; Q9MAL0; -.
DR OMA; LHEDMEN; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9MAL0; -.
DR BioCyc; ARA:AT1G44980-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9MAL0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAL0; differential.
DR Genevisible; Q9MAL0; AT.
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; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase; Glycoprotein; Hydrolase; Reference proteome.
FT CHAIN 1..246
FT /note="Putative pectinesterase 57"
FT /id="PRO_0000371705"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 204
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 246 AA; 27743 MW; 278E69BBC60B7B39 CRC64;
MAMIGVMEDS KLHEDMENDM LGDLTSRARE ALALFISISL RDNTELNLVV PNGPSWLSHV
DKKDLYLNDE TLKKITDILV AKDVTGNYNI VNVAIAAAPQ HSQKRFVIYI KTSIYVEIVV
IGNMKSNLTL IADGQDSTII TFNLSSSNSK RTFNTATFAS NGDGFIRVDM CFRNTTWPVK
GPVVTLRVNG DMSIIYRCRV EEYQDALYPH KNRQCYREYF LMDTVDFICG NAAAVFQFCQ
IVHMDG
