PME19_ARATH
ID PME19_ARATH Reviewed; 524 AA.
AC Q84JX1; Q9LPX7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 19;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 19;
DE AltName: Full=Pectin methylesterase inhibitor 19;
DE Includes:
DE RecName: Full=Pectinesterase 19;
DE Short=PE 19;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 19;
DE Short=AtPME19;
DE AltName: Full=Pectin methylesterase 5;
DE Short=AtPME5;
DE Flags: Precursor;
GN Name=PME19; Synonyms=ARATH5; OrderedLocusNames=At1g11590;
GN ORFNames=T23J18.25;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 siliques, but not in flower buds.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expression restricted to early to mid-stage of
CC silique development. Not found in vegetative stage. Expressed in the
CC micropyle area of the ovule just after fertilization.
CC {ECO:0000269|PubMed:16622707}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16638.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011661; AAF16638.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28756.1; -; Genomic_DNA.
DR EMBL; BT003962; AAO42007.1; -; mRNA.
DR EMBL; BT004987; AAO50520.1; -; mRNA.
DR RefSeq; NP_172625.3; NM_101032.3.
DR AlphaFoldDB; Q84JX1; -.
DR SMR; Q84JX1; -.
DR BioGRID; 22942; 1.
DR STRING; 3702.AT1G11590.1; -.
DR PaxDb; Q84JX1; -.
DR PRIDE; Q84JX1; -.
DR ProteomicsDB; 236573; -.
DR EnsemblPlants; AT1G11590.1; AT1G11590.1; AT1G11590.
DR GeneID; 837702; -.
DR Gramene; AT1G11590.1; AT1G11590.1; AT1G11590.
DR KEGG; ath:AT1G11590; -.
DR Araport; AT1G11590; -.
DR TAIR; locus:2200121; AT1G11590.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR InParanoid; Q84JX1; -.
DR OMA; MMESTKD; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q84JX1; -.
DR BioCyc; ARA:AT1G11590-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q84JX1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84JX1; baseline and differential.
DR Genevisible; Q84JX1; AT.
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; 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; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
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 PROSITE; PS00800; PECTINESTERASE_1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..524
FT /note="Probable pectinesterase/pectinesterase inhibitor 19"
FT /id="PRO_0000371675"
FT REGION 23..172
FT /note="Pectinesterase inhibitor 19"
FT REGION 215..510
FT /note="Pectinesterase 19"
FT ACT_SITE 343
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 364
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 342
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 357..377
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 58692 MW; 56405865F937BA1D CRC64;
MLVKVFSFFI LMITMVVIGV SKEYCDDKQS CQNFLLELKA GSSSLSEIRR RDLLIIVLKN
SVRRIDMVMI GVMDDTKQHE EMENDLLGVK EDTKLFEEMM ESTKDRMIRS VEELLGGEFP
NRGSYENVHT WLSSVLTSYI TCIDEIGEGA YKRRVEPKLE DLISRARIAL ALFISISPRD
NTELISVIPN SPSWLFHVDK KDLYLNAEAL KKIADVVVAK DGTGKYSTVN AAIAAAPQHS
QKRFVIYIKT GIYDEIVVIE NTKPNLTLIG DGQDLTIITS NLSASNVRRT FNTATVASNG
NGFIGVDMCF RNTAGPAKGP AVALRVSGDM SVIYRCRVEG YQDALYPHSD RQFYRECFIT
GTVDFICGNA VAVFQFCQIV ARQPKMGQSN VITAQSRAFK DIYSGFTIQK CNITASSDLD
TTTVKTYLGR PWRIFSTVAV MQSFIGDLVD PAGWTPWEGE TGLSTLHYRE YQNRGPGAVT
SRRVKWSGFK VMKDPKQATE FTVAKLLDGE TWLKETRIPY ESGL
