PME48_ARATH
ID PME48_ARATH Reviewed; 361 AA.
AC Q9LY19; Q56WP9; Q8LAH3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable pectinesterase 48;
DE Short=PE 48;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 48;
DE Short=AtPME48;
DE Flags: Precursor;
GN Name=PME48; Synonyms=ARATH48; OrderedLocusNames=At5g07410;
GN ORFNames=T2I1.120;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-361.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) 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 -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65347.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD94545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB87930.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL163912; CAB87930.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91154.1; -; Genomic_DNA.
DR EMBL; AY087811; AAM65347.1; ALT_INIT; mRNA.
DR EMBL; AK221986; BAD94545.1; ALT_INIT; mRNA.
DR PIR; T49880; T49880.
DR RefSeq; NP_568181.1; NM_120823.4.
DR AlphaFoldDB; Q9LY19; -.
DR SMR; Q9LY19; -.
DR STRING; 3702.AT5G07410.1; -.
DR PaxDb; Q9LY19; -.
DR PRIDE; Q9LY19; -.
DR ProteomicsDB; 234745; -.
DR EnsemblPlants; AT5G07410.1; AT5G07410.1; AT5G07410.
DR GeneID; 830632; -.
DR Gramene; AT5G07410.1; AT5G07410.1; AT5G07410.
DR KEGG; ath:AT5G07410; -.
DR Araport; AT5G07410; -.
DR TAIR; locus:2183334; AT5G07410.
DR eggNOG; ENOG502R3C8; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q9LY19; -.
DR OMA; MRISGNM; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9LY19; -.
DR BioCyc; ARA:AT5G07410-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9LY19; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY19; baseline and differential.
DR Genevisible; Q9LY19; 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:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0030599; F:pectinesterase activity; IMP:TAIR.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
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 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..361
FT /note="Probable pectinesterase 48"
FT /id="PRO_0000371696"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 48
FT /note="A -> V (in Ref. 3; AAM65347)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="H -> P (in Ref. 3; AAM65347)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="K -> N (in Ref. 3; AAM65347)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="G -> V (in Ref. 3; AAM65347)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="C -> R (in Ref. 3; AAM65347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39337 MW; C0663F0A5FAB2D3E CRC64;
MRYTNVSILL GMLVIFVSPM VFADDLTPIP EGKPQVVQWF NTHVGPLAQR KGLDPALVAA
EAAPRIINVN PKGGEFKTLT DAIKSVPAGN TKRVIIKMAH GEYREKVTID RNKPFITLMG
QPNAMPVITY DGTAAKYGTV DSASLIILSD YFMAVNIVVK NTAPAPDGKT KGAQALSMRI
SGNFAAFYNC KFYGFQDTIC DDTGNHFFKD CYVEGTFDFI FGSGTSMYLG TQLHVVGDGI
RVIAAHAGKS AEEKSGYSFV HCKVTGTGGG IYLGRAWMSH PKVVYAYTEM TSVVNPTGWQ
ENKTPAHDKT VFYGEYKCSG PGSHKAKRVP FTQDIDDKEA NCFLSLGYIQ GSKWLLPPPA
L
