ID PME55_ARATH Reviewed; 330 AA.
AC Q3E9D3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 51.
DE RecName: Full=Probable pectinesterase 55;
DE Short=PE 55;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 55;
DE Short=AtPME55;
DE Flags: Precursor;
GN Name=PME55; Synonyms=ARATH55; OrderedLocusNames=At5g18990;
GN ORFNames=T16G12.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
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.,
RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA 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.,
RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Pectin + n H(2)O = n methanol + pectate.
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-
CC D-gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall (By similarity).
CC -!- SIMILARITY: Belongs to the pectinesterase family.
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DR EMBL; AC068809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92636.1; -; Genomic_DNA.
DR IPI; IPI00532537; -.
DR RefSeq; NP_197400.1; NM_121904.1.
DR UniGene; At.54913; -.
DR ProteinModelPortal; Q3E9D3; -.
DR SMR; Q3E9D3; 29-324.
DR EnsemblPlants; AT5G18990.1; AT5G18990.1; AT5G18990.
DR GeneID; 832017; -.
DR KEGG; ath:AT5G18990; -.
DR TAIR; At5g18990; -.
DR eggNOG; COG4677; -.
DR HOGENOM; HOG000217409; -.
DR InParanoid; Q3E9D3; -.
DR OMA; PINNTHW; -.
DR PhylomeDB; Q3E9D3; -.
DR ProtClustDB; PLN02497; -.
DR UniPathway; UPA00545; UER00823.
DR Genevestigator; Q3E9D3; -.
DR GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
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; IEA:EC.
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; Pectin_lyas_like; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; FALSE_NEG.
DR PROSITE; PS00503; PECTINESTERASE_2; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Complete proteome; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 24 Potential.
FT CHAIN 25 330 Probable pectinesterase 55.
FT /FTId=PRO_0000371703.
FT ACT_SITE 161 161 Proton donor (By similarity).
FT ACT_SITE 182 182 Nucleophile (By similarity).
FT BINDING 243 243 Substrate (By similarity).
FT BINDING 245 245 Substrate (By similarity).
FT SITE 160 160 Transition state stabilizer (By
FT similarity).
FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 52 52 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 257 257 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 292 292 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 330 AA; 36460 MW; BFB86E7CD3D43263 CRC64;
MGTHRIILGL AALCCFCLPH LIEAKPFEVI VDQSGHGNFT TIQKAIDSVP INNTHWFFIN
VKAGLYREKI TIPQKKPFIV IVGAGKRSTR VEWDDHASLA QSPTFATLAD NTVVKKITFA
NSYNFPSNGK INKNPRVPAV AAFIGGDKSA FYSVGFAGIQ DTLWDSDGRH YFHRCTIQGA
VDFILGSGQS IYQSCVIQVL GGQLGPGVTG YITAQGRTNA NDANGFVFIN CLVHGFGKAY
LGRAWRPYSR VIFYNSNLTD VVDPLGWWEW NYQGYEKQLT YAEHGCFGSG SNTSRRAKWV
KKLSASAVQH LADLSFINRG GWVEDLPIRV
//
