PME24_ARATH
ID PME24_ARATH Reviewed; 561 AA.
AC Q9SG77;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative pectinesterase/pectinesterase inhibitor 24;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 24;
DE AltName: Full=Pectin methylesterase inhibitor 24;
DE Includes:
DE RecName: Full=Pectinesterase 24;
DE Short=PE 24;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 24;
DE Short=AtPME24;
GN Name=PME24; Synonyms=ARATH24; OrderedLocusNames=At3g10710;
GN ORFNames=T7M13.21;
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: 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; AC011708; AAF19578.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74945.1; -; Genomic_DNA.
DR RefSeq; NP_187682.1; NM_111907.2.
DR AlphaFoldDB; Q9SG77; -.
DR SMR; Q9SG77; -.
DR STRING; 3702.AT3G10710.1; -.
DR PaxDb; Q9SG77; -.
DR PRIDE; Q9SG77; -.
DR ProteomicsDB; 234778; -.
DR EnsemblPlants; AT3G10710.1; AT3G10710.1; AT3G10710.
DR GeneID; 820240; -.
DR Gramene; AT3G10710.1; AT3G10710.1; AT3G10710.
DR KEGG; ath:AT3G10710; -.
DR Araport; AT3G10710; -.
DR TAIR; locus:2103227; AT3G10710.
DR eggNOG; ENOG502QVDS; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR InParanoid; Q9SG77; -.
DR OMA; YGKVDEH; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9SG77; -.
DR BioCyc; ARA:AT3G10710-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9SG77; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SG77; baseline and differential.
DR Genevisible; Q9SG77; 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; 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 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 3: Inferred from homology;
KW Aspartyl esterase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..561
FT /note="Putative pectinesterase/pectinesterase inhibitor 24"
FT /id="PRO_0000370187"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 64..211
FT /note="Pectinesterase inhibitor 24"
FT REGION 255..548
FT /note="Pectinesterase 24"
FT ACT_SITE 383
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 404
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 468
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 SITE 382
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 397..417
FT /evidence="ECO:0000250"
SQ SEQUENCE 561 AA; 62103 MW; 67136DD2C6AD074B CRC64;
MSSPYGKVDE REHVRLEARR KTRKNIAIIA VSLVILAGIV IGAVFGTMAH KKSPETVETN
NNGDSISVSV KAVCDVTLHK EKCFETLGSA PNASSLNPEE LFRYAVKITI AEVSKAINAF
SSSLGDEKNN ITMNACAELL DLTIDNLNNT LTSSSNGDVT VPELVDDLRT WLSSAGTYQR
TCVETLAPDM RPFGESHLKN STELTSNALA IITWLGKIAD SFKLRRRLLT TADVEVDFHA
GRRLLQSTDL RKVADIVVAK DGSGKYRTIK RALQDVPEKS EKRTIIYVKK GVYFENVKVE
KKMWNVIVVG DGESKSIVSG RLNVIDGTPT FKTATFAVFG KGFMARDMGF INTAGPSKHQ
AVALMVSADL TAFYRCTMNA YQDTLYVHAQ RQFYRECTII GTVDFIFGNS ASVLQSCRIL
PRRPMKGQQN TITAQGRTDP NMNTGISIHR CNISPLGDLT DVMTFLGRPW KNFSTTVIMD
SYLHGFIDRK GWLPWTGDSA PDTIFYGEYK NTGPGASTKN RVKWKGLRFL STKEANRFTV
KPFIDGGRWL PATKVPFRSG L
