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RecName: Full=Probable pectinesterase/pectinesterase inhibitor 51; Includes: RecName: Full=Pectinesterase inhibitor 51; AltName: Full=Pectin methylesterase inhibitor 51; Includes: RecName: Full=Pectinesterase 51; Short=PE 51; AltName: Full=Pectin methylesteras...

UniProtKB/Swiss-Prot: Q9LXD9.1

Identical Proteins FASTA Graphics 

LOCUS       PME51_ARATH              551 aa            linear   PLN 27-NOV-2024
DEFINITION  RecName: Full=Probable pectinesterase/pectinesterase inhibitor 51;
            Includes: RecName: Full=Pectinesterase inhibitor 51; AltName:
            Full=Pectin methylesterase inhibitor 51; Includes: RecName:
            Full=Pectinesterase 51; Short=PE 51; AltName: Full=Pectin
            methylesterase 51; Short=AtPME51; Flags: Precursor.
ACCESSION   Q9LXD9
VERSION     Q9LXD9.1
DBSOURCE    UniProtKB: locus PME51_ARATH, accession Q9LXD9;
            class: standard.
            extra accessions:Q9FXW9
            created: May 5, 2009.
            sequence updated: Oct 1, 2000.
            annotation updated: Nov 27, 2024.
            xrefs: AB020752.1, BAB09534.1, AL353994.1, CAB89354.1, CP002688.1,
            AED91443.1, AY070093.1, AAL49830.1, BT006059.1, AAP04044.1, T49922,
            NP_001331158.1, NP_196538.1
            xrefs (non-sequence databases): AlphaFoldDB:Q9LXD9, SMR:Q9LXD9,
            STRING:3702.Q9LXD9, GlyCosmos:Q9LXD9, iPTMnet:Q9LXD9,
            PaxDb:3702-AT5G09760.1, EnsemblPlants:AT5G09760.1,
            EnsemblPlants:AT5G09760.1, EnsemblPlants:AT5G09760, GeneID:830836,
            Gramene:AT5G09760.1, KEGG:ath:AT5G09760, Araport:AT5G09760,
            TAIR:AT5G09760, eggNOG:ENOG502QW0X, HOGENOM:CLU_012243_9_3_1,
            InParanoid:Q9LXD9, OrthoDB:668039at2759, PhylomeDB:Q9LXD9,
            UniPathway:UPA00545, PRO:PR:Q9LXD9, Proteomes:UP000006548,
            ExpressionAtlas:Q9LXD9, GO:0005576, GO:0004857, GO:0030599,
            GO:0042545, GO:0045490, CDD:cd15798, FunFam:2.160.20.10:FF:000001,
            FunFam:1.20.140.40:FF:000021, Gene3D:1.20.140.40,
            Gene3D:2.160.20.10, InterPro:IPR035513, InterPro:IPR012334,
            InterPro:IPR011050, InterPro:IPR000070, InterPro:IPR006501,
            NCBIfam:TIGR01614, PANTHER:PTHR31707, PANTHER:PTHR31707:SF271,
            Pfam:PF01095, Pfam:PF04043, SMART:SM00856, SUPFAM:SSF51126,
            SUPFAM:SSF101148
KEYWORDS    Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
            Disulfide bond; Glycoprotein; Hydrolase; Reference proteome;
            Secreted; Signal.
SOURCE      Arabidopsis thaliana (thale cress)
  ORGANISM  Arabidopsis thaliana
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
            Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
            Camelineae; Arabidopsis.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Kaneko,T., Katoh,T., Sato,S., Nakamura,Y., Asamizu,E., Kotani,H.,
            Miyajima,N. and Tabata,S.
  TITLE     Structural analysis of Arabidopsis thaliana chromosome 5. IX.
            Sequence features of the regions of 1,011,550 bp covered by
            seventeen P1 and TAC clones
  JOURNAL   DNA Res 6 (3), 183-195 (1999)
   PUBMED   10470850
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=cv. Columbia
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Tabata,S., Kaneko,T., Nakamura,Y., Kotani,H., Kato,T., Asamizu,E.,
            Miyajima,N., Sasamoto,S., Kimura,T., Hosouchi,T., Kawashima,K.,
            Kohara,M., Matsumoto,M., Matsuno,A., Muraki,A., Nakayama,S.,
            Nakazaki,N., Naruo,K., Okumura,S., Shinpo,S., Takeuchi,C., Wada,T.,
            Watanabe,A., Yamada,M., Yasuda,M., Sato,S., de la Bastide,M.,
            Huang,E., Spiegel,L., Gnoj,L., O'Shaughnessy,A., Preston,R.,
            Habermann,K., Murray,J., Johnson,D., Rohlfing,T., Nelson,J.,
            Stoneking,T., Pepin,K., Spieth,J., Sekhon,M., Armstrong,J.,
            Becker,M., Belter,E., Cordum,H., Cordes,M., Courtney,L.,
            Courtney,W., Dante,M., Du,H., Edwards,J., Fryman,J., Haakensen,B.,
            Lamar,E., Latreille,P., Leonard,S., Meyer,R., Mulvaney,E.,
            Ozersky,P., Riley,A., Strowmatt,C., Wagner-McPherson,C., Wollam,A.,
            Yoakum,M., Bell,M., Dedhia,N., Parnell,L., Shah,R., Rodriguez,M.,
            See,L.H., Vil,D., Baker,J., Kirchoff,K., Toth,K., King,L.,
            Bahret,A., Miller,B., Marra,M., Martienssen,R., McCombie,W.R.,
            Wilson,R.K., Murphy,G., Bancroft,I., Volckaert,G., Wambutt,R.,
            Dusterhoft,A., Stiekema,W., Pohl,T., Entian,K.D., Terryn,N.,
            Hartley,N., Bent,E., Johnson,S., Langham,S.A., McCullagh,B.,
            Robben,J., Grymonprez,B., Zimmermann,W., Ramsperger,U., Wedler,H.,
            Balke,K., Wedler,E., Peters,S., van Staveren,M., Dirkse,W.,
            Mooijman,P., Lankhorst,R.K., Weitzenegger,T., Bothe,G., Rose,M.,
            Hauf,J., Berneiser,S., Hempel,S., Feldpausch,M., Lamberth,S.,
            Villarroel,R., Gielen,J., Ardiles,W., Bents,O., Lemcke,K.,
            Kolesov,G., Mayer,K., Rudd,S., Schoof,H., Schueller,C.,
            Zaccaria,P., Mewes,H.W., Bevan,M. and Fransz,P.
  CONSRTM   Kazusa DNA Research Institute; Cold Spring Harbor and Washington
            University in St Louis Sequencing Consortium; European Union
            Arabidopsis Genome Sequencing Consortium
  TITLE     Sequence and analysis of chromosome 5 of the plant Arabidopsis
            thaliana
  JOURNAL   Nature 408 (6814), 823-826 (2000)
   PUBMED   11130714
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=cv. Columbia
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Cheng,C.Y., Krishnakumar,V., Chan,A.P., Thibaud-Nissen,F.,
            Schobel,S. and Town,C.D.
  TITLE     Araport11: a complete reannotation of the Arabidopsis thaliana
            reference genome
  JOURNAL   Plant J 89 (4), 789-804 (2017)
   PUBMED   27862469
  REMARK    GENOME REANNOTATION.;
            STRAIN=cv. Columbia
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Yamada,K., Lim,J., Dale,J.M., Chen,H., Shinn,P., Palm,C.J.,
            Southwick,A.M., Wu,H.C., Kim,C., Nguyen,M., Pham,P., Cheuk,R.,
            Karlin-Newmann,G., Liu,S.X., Lam,B., Sakano,H., Wu,T., Yu,G.,
            Miranda,M., Quach,H.L., Tripp,M., Chang,C.H., Lee,J.M., Toriumi,M.,
            Chan,M.M., Tang,C.C., Onodera,C.S., Deng,J.M., Akiyama,K.,
            Ansari,Y., Arakawa,T., Banh,J., Banno,F., Bowser,L., Brooks,S.,
            Carninci,P., Chao,Q., Choy,N., Enju,A., Goldsmith,A.D., Gurjal,M.,
            Hansen,N.F., Hayashizaki,Y., Johnson-Hopson,C., Hsuan,V.W.,
            Iida,K., Karnes,M., Khan,S., Koesema,E., Ishida,J., Jiang,P.X.,
            Jones,T., Kawai,J., Kamiya,A., Meyers,C., Nakajima,M., Narusaka,M.,
            Seki,M., Sakurai,T., Satou,M., Tamse,R., Vaysberg,M.,
            Wallender,E.K., Wong,C., Yamamura,Y., Yuan,S., Shinozaki,K.,
            Davis,R.W., Theologis,A. and Ecker,J.R.
  TITLE     Empirical analysis of transcriptional activity in the Arabidopsis
            genome
  JOURNAL   Science 302 (5646), 842-846 (2003)
   PUBMED   14593172
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=cv. Columbia
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Markovic,O. and Janecek,S.
  TITLE     Pectin methylesterases: sequence-structural features and
            phylogenetic relationships
  JOURNAL   Carbohydr Res 339 (13), 2281-2295 (2004)
   PUBMED   15337457
  REMARK    GENE FAMILY, AND NOMENCLATURE.
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Louvet,R., Cavel,E., Gutierrez,L., Guenin,S., Roger,D., Gillet,F.,
            Guerineau,F. and Pelloux,J.
  TITLE     Comprehensive expression profiling of the pectin methylesterase
            gene family during silique development in Arabidopsis thaliana
  JOURNAL   Planta 224 (4), 782-791 (2006)
   PUBMED   16622707
  REMARK    TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
COMMENT     On or before May 8, 2009 this sequence version replaced
            gi:75173143, gi:11279195.
            [FUNCTION] Acts in the modification of cell walls via
            demethylesterification of cell wall pectin. {ECO:0000250}.
            [CATALYTIC ACTIVITY] Reaction=[(1->4)-alpha-D-galacturonosyl methyl
            ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n methanol
            + n H(+); Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570,
            Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523;
            EC=3.1.1.11.
            [PATHWAY] Glycan metabolism; pectin degradation;
            2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
            [SUBCELLULAR LOCATION] Secreted, cell wall {ECO:0000250}.
            [TISSUE SPECIFICITY] Expressed in siliques.
            {ECO:0000269|PubMed:16622707}.
            [DEVELOPMENTAL STAGE] Expressed throughout silique development.
            {ECO:0000269|PubMed:16622707}.
            [MISCELLANEOUS] The PMEI region may act as an autoinhibitory domain
            and prevent untimely PME activity during transport.
            [SIMILARITY] In the N-terminal section; belongs to the PMEI family.
            {ECO:0000305}.
            [SIMILARITY] In the C-terminal section; belongs to the
            pectinesterase family. {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=BAB09534.1; Type=Erroneous initiation;
            Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Arabidopsis thaliana"
                     /db_xref="taxon:3702"
     gene            1..551
                     /gene="PME51"
                     /locus_tag="At5g09760"
                     /gene_synonym="ARATH51"
                     /gene_synonym="F17I14.50"
     Protein         1..551
                     /product="Probable pectinesterase/pectinesterase inhibitor
                     51"
                     /EC_number="3.1.1.11"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..20
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          21..551
                     /region_name="Mature chain"
                     /note="Probable pectinesterase/pectinesterase inhibitor
                     51. /id=PRO_0000371699."
     Region          30..551
                     /region_name="PLN02708"
                     /note="Probable pectinesterase/pectinesterase inhibitor"
                     /db_xref="CDD:215379"
     Region          39..189
                     /region_name="Region of interest in the sequence"
                     /note="Pectinesterase inhibitor 51."
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          240..544
                     /region_name="Region of interest in the sequence"
                     /note="Pectinesterase 51."
     Site            369
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250."
     Site            370
                     /site_type="active"
                     /note="Proton donor; for pectinesterase activity.
                     /evidence=ECO:0000250."
     Bond            bond(384,404)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            391
                     /site_type="active"
                     /note="Nucleophile; for pectinesterase activity.
                     /evidence=ECO:0000250."
     Site            445
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN      
        1 mssilillfs lflfsspsss srhhhhhnsg dtspvnpsss laaqirlacn atrypdqcvs
       61 slseqgrvpp dpkpiqiihs aisfsfqnlk taqskiksiv dssvgnlnrt naantclqll
      121 tysehrtqst dqaltrgkik darawmsaal vyqydswsal kyvndtsqvg etmsfldgli
      181 hvtsnalsmm vsydnfgdnv aswtypater dgfwektgpg lgldpstgln lgfpsglked
      241 vtvckdgkcg yktvqdavna apedngmrkf vikisegvye envivpfekk nvvfigdgmg
      301 ktvitgslna gmpgittynt atvgvvgdgf mardltfqnt agpdahqava frsdsdfsli
      361 enceflgnqd tlyahglrqf ykncriqgnv dfifgnsaav fqdceiliap rqinpekgek
      421 navtaqgrid psqstgfvfl nclingteey mklfkanpkv hknflgrpwk dysrtvfigc
      481 nlealitpdg wlpwsgdfal ktlyygeskn tgpgsdrsqr vswssqipde hvhvysvanf
      541 iqadewasms a
//
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