PME6_ARATH
ID PME6_ARATH Reviewed; 554 AA.
AC O49298;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 6;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 6;
DE AltName: Full=Pectin methylesterase inhibitor 6;
DE Includes:
DE RecName: Full=Pectinesterase 6;
DE Short=PE 6;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 6;
DE Short=AtPME6;
DE Flags: Precursor;
GN Name=PME6; Synonyms=ARATH6; OrderedLocusNames=At1g23200; ORFNames=T26J12.4;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA Micheli F., Holliger C., Goldberg R., Richard L.;
RT "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT member of a gene family comprising at least 12 genes in Arabidopsis
RT thaliana.";
RL Gene 220:13-20(1998).
RN [6]
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 [7]
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 rosette leaves, flower and siliques.
CC {ECO:0000269|PubMed:16622707, ECO:0000269|PubMed:9767082}.
CC -!- DEVELOPMENTAL STAGE: Low expression in vegetative and flower stages. No
CC expression in young siliques but highly expressed in older siliques.
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}.
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DR EMBL; AC002311; AAC00600.1; -; Genomic_DNA.
DR EMBL; AC005292; AAF86993.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30354.1; -; Genomic_DNA.
DR EMBL; AY065263; AAL38739.1; -; mRNA.
DR EMBL; AY091325; AAM14264.1; -; mRNA.
DR EMBL; AK227025; BAE99088.1; -; mRNA.
DR PIR; C86366; C86366.
DR RefSeq; NP_173733.1; NM_102168.4.
DR AlphaFoldDB; O49298; -.
DR SMR; O49298; -.
DR STRING; 3702.AT1G23200.1; -.
DR iPTMnet; O49298; -.
DR PaxDb; O49298; -.
DR PRIDE; O49298; -.
DR ProteomicsDB; 226273; -.
DR EnsemblPlants; AT1G23200.1; AT1G23200.1; AT1G23200.
DR GeneID; 838928; -.
DR Gramene; AT1G23200.1; AT1G23200.1; AT1G23200.
DR KEGG; ath:AT1G23200; -.
DR Araport; AT1G23200; -.
DR TAIR; locus:2201230; AT1G23200.
DR eggNOG; ENOG502QTQV; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; O49298; -.
DR OMA; HFITSCK; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; O49298; -.
DR BioCyc; ARA:AT1G23200-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:O49298; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49298; baseline and differential.
DR Genevisible; O49298; 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; IMP:TAIR.
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; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
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 TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..554
FT /note="Probable pectinesterase/pectinesterase inhibitor 6"
FT /id="PRO_0000371663"
FT REGION 29..183
FT /note="Pectinesterase inhibitor 6"
FT REGION 250..540
FT /note="Pectinesterase 6"
FT ACT_SITE 380
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 401
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 327
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 379
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 394..414
FT /evidence="ECO:0000250"
SQ SEQUENCE 554 AA; 61270 MW; C2EAC4FDC2CAF387 CRC64;
MDHKILLTPP KSLYTKCIIT IIYVVSISHL NAHFITSCKQ TPYPSVCDHH MSNSPLKTLD
DQTDGFTFHD LVVSSTMDQA VQLHRLVSSL KQHHSLHKHA TSALFDCLEL YEDTIDQLNH
SRRSYGQYSS PHDRQTSLSA AIANQDTCRN GFRDFKLTSS YSKYFPVQFH RNLTKSISNS
LAVTKAAAEA EAVAEKYPST GFTKFSKQRS SAGGGSHRRL LLFSDEKFPS WFPLSDRKLL
EDSKTTAKAD LVVAKDGSGH YTSIQQAVNA AAKLPRRNQR LVIYVKAGVY RENVVIKKSI
KNVMVIGDGI DSTIVTGNRN VQDGTTTFRS ATFAVSGNGF IAQGITFENT AGPEKHQAVA
LRSSSDFSVF YACSFKGYQD TLYLHSSRQF LRNCNIYGTV DFIFGDATAI LQNCNIYARK
PMSGQKNTIT AQSRKEPDET TGFVIQSSTV ATASETYLGR PWRSHSRTVF MKCNLGALVS
PAGWLPWSGS FALSTLYYGE YGNTGAGASV SGRVKWPGYH VIKTVTEAEK FTVENFLDGN
YWITATGVPV NDGL
