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
//