PME23_ARATH
ID PME23_ARATH Reviewed; 568 AA.
AC Q8GXA1; A4FVQ5; Q9M7Y9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 23;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 23;
DE AltName: Full=Pectin methylesterase inhibitor 23;
DE Includes:
DE RecName: Full=Pectinesterase 23;
DE Short=PE 23;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 23;
DE Short=AtPME23;
DE Flags: Precursor;
GN Name=PME23; Synonyms=ARATH23; OrderedLocusNames=At3g06830;
GN ORFNames=F3E22.3;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) 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.
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 mature pollen grains in the anthers
CC and on the stigma. Found in pollen tubes within the style.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63815.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023912; AAF63815.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74464.1; -; Genomic_DNA.
DR EMBL; AK118345; BAC42959.2; -; mRNA.
DR EMBL; BT030353; ABO38766.1; -; mRNA.
DR RefSeq; NP_187339.2; NM_111563.4.
DR AlphaFoldDB; Q8GXA1; -.
DR SMR; Q8GXA1; -.
DR STRING; 3702.AT3G06830.1; -.
DR PaxDb; Q8GXA1; -.
DR PRIDE; Q8GXA1; -.
DR ProteomicsDB; 226206; -.
DR EnsemblPlants; AT3G06830.1; AT3G06830.1; AT3G06830.
DR GeneID; 819867; -.
DR Gramene; AT3G06830.1; AT3G06830.1; AT3G06830.
DR KEGG; ath:AT3G06830; -.
DR Araport; AT3G06830; -.
DR TAIR; locus:2083308; AT3G06830.
DR eggNOG; ENOG502R6WA; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q8GXA1; -.
DR OMA; HGCHITG; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q8GXA1; -.
DR BioCyc; ARA:AT3G06830-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q8GXA1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GXA1; baseline and differential.
DR Genevisible; Q8GXA1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
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 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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..568
FT /note="Probable pectinesterase/pectinesterase inhibitor 23"
FT /id="PRO_0000371679"
FT REGION 45..198
FT /note="Pectinesterase inhibitor 23"
FT REGION 251..548
FT /note="Pectinesterase 23"
FT ACT_SITE 386
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 407
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 333
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 475
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 SITE 385
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 400..420
FT /evidence="ECO:0000250"
FT CONFLICT 107
FT /note="K -> E (in Ref. 3; BAC42959)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="V -> A (in Ref. 3; BAC42959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 61886 MW; FE92C797055361A7 CRC64;
MGSDGDKKKK FIVAGSVSGF LVIMVVSVAV VTSKHSPKDD ENHIRKTTKA VQAVCAPTDF
KDTCVNSLMG ASPDSDDPVD LIKLGFKVTI KSINESLEKA SGDIKAKADK NPEAKGAFEL
CEKLMIDAID DLKKCMDHGF SVDQIEVFVE DLRVWLSGSI AFQQTCMDSF GEIKSNLMQD
MLKIFKTSRE LSSNSLAMVT RISTLIPNSN LTGLTGALAK YARKLLSTED SIPTWVGPEA
RRLMAAQGGG PGPVKANAVV AQDGTGQFKT ITDALNAVPK GNKVPFIIHI KEGIYKEKVT
VTKKMPHVTF IGDGPNKTLI TGSLNFGIGK VKTFLTATIT IEGDHFTAKN IGIENTAGPE
GGQAVALRVS ADYAVFHSCQ IDGHQDTLYV HSHRQFYRDC TVSGTVDFIF GDAKCILQNC
KIVVRKPNKG QTCMVTAQGR SNVRESTGLV LHGCHITGDP AYIPMKSVNK AYLGRPWKEF
SRTIIMKTTI DDVIDPAGWL PWSGDFALKT LYYAEHMNTG PGSNQAQRVK WPGIKKLTPQ
DALLYTGDRF LRGDTWIPQT QVPYTAKV
