PME22_ARATH
ID PME22_ARATH Reviewed; 543 AA.
AC Q9M9W7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative pectinesterase/pectinesterase inhibitor 22;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 22;
DE AltName: Full=Pectin methylesterase inhibitor 22;
DE Includes:
DE RecName: Full=Pectinesterase 22;
DE Short=PE 22;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 22;
DE Short=AtPME22;
DE Flags: Precursor;
GN Name=PME22; Synonyms=ARATH22; OrderedLocusNames=At3g05620;
GN ORFNames=F18C1.11;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 -!- 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; AC011620; AAF26135.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74267.1; -; Genomic_DNA.
DR RefSeq; NP_187213.1; NM_111435.2.
DR AlphaFoldDB; Q9M9W7; -.
DR SMR; Q9M9W7; -.
DR STRING; 3702.AT3G05620.1; -.
DR MetOSite; Q9M9W7; -.
DR PaxDb; Q9M9W7; -.
DR PRIDE; Q9M9W7; -.
DR ProteomicsDB; 234680; -.
DR EnsemblPlants; AT3G05620.1; AT3G05620.1; AT3G05620.
DR GeneID; 819728; -.
DR Gramene; AT3G05620.1; AT3G05620.1; AT3G05620.
DR KEGG; ath:AT3G05620; -.
DR Araport; AT3G05620; -.
DR TAIR; locus:2078047; AT3G05620.
DR eggNOG; ENOG502QU1M; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q9M9W7; -.
DR OMA; WSMLEMN; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9M9W7; -.
DR BioCyc; ARA:AT3G05620-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9M9W7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9W7; baseline and differential.
DR Genevisible; Q9M9W7; 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 3: Inferred from homology;
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..543
FT /note="Putative pectinesterase/pectinesterase inhibitor 22"
FT /id="PRO_0000371678"
FT REGION 38..197
FT /note="Pectinesterase inhibitor 22"
FT REGION 240..527
FT /note="Pectinesterase 22"
FT ACT_SITE 368
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 389
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 315
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 367
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 382..402
FT /evidence="ECO:0000250"
SQ SEQUENCE 543 AA; 60806 MW; 012165468B4C084F CRC64;
MGITTALLLV MLMSVHTSSY ETTILKPYKE DNFRSLVAKA CQFIDAHELC VSNIWTHVKE
SGHGLNPHSV LRAAVKEAHD KAKLAMERIP TVMMLSIRSR EQVAIEDCKE LVGFSVTELA
WSMLEMNKLH GGGGIDLDDG SHDAAAAGGN LKTWLSAAMS NQDTCLEGFE GTERKYEELI
KGSLRQVTQL VSNVLDMYTQ LNALPFKASR NESVIASPEW LTETDESLMM RHDPSVMHPN
TVVAIDGKGK YRTINEAINE APNHSTKRYV IYVKKGVYKE NIDLKKKKTN IMLVGDGIGQ
TIITGDRNFM QGLTTFRTAT VAVSGRGFIA KDITFRNTAG PQNRQAVALR VDSDQSAFYR
CSVEGYQDTL YAHSLRQFYR DCEIYGTIDF IFGNGAAVLQ NCKIYTRVPL PLQKVTITAQ
GRKSPNQNTG FVIQNSYVLA TQPTYLGRPW KLYSRTVYMN TYMSQLVQPR GWLEWFGNFA
LDTLWYGEYN NIGPGWRSSG RVKWPGYHIM DKRTALSFTV GSFIDGRRWL PATGVTFTAG
LAN
