PME2_ARATH
ID PME2_ARATH Reviewed; 587 AA.
AC Q42534; Q9SSB0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Pectinesterase 2;
DE Short=PE 2;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 2;
DE Short=AtPME2;
DE Flags: Precursor;
GN Name=PME2; Synonyms=ARATH8; OrderedLocusNames=At1g53830; ORFNames=T18A20.6;
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 [GENOMIC DNA] OF 6-587.
RX PubMed=8666246; DOI=10.1016/0378-1119(95)00766-0;
RA Richard L., Qin L.X., Goldberg R.;
RT "Clustered genes within the genome of Arabidopsis thaliana encoding pectin
RT methylesterase-like enzymes.";
RL Gene 170:207-211(1996).
RN [5]
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 [6]
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:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds.
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; AC009324; AAF02856.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33007.1; -; Genomic_DNA.
DR EMBL; AF361637; AAK32805.1; -; mRNA.
DR EMBL; AY133609; AAM91439.1; -; mRNA.
DR EMBL; U25649; AAC50023.1; -; Genomic_DNA.
DR PIR; D96578; D96578.
DR PIR; PC4168; PC4168.
DR RefSeq; NP_175786.1; NM_104260.5.
DR AlphaFoldDB; Q42534; -.
DR SMR; Q42534; -.
DR BioGRID; 27045; 1.
DR STRING; 3702.AT1G53830.1; -.
DR iPTMnet; Q42534; -.
DR PaxDb; Q42534; -.
DR PRIDE; Q42534; -.
DR ProteomicsDB; 234980; -.
DR EnsemblPlants; AT1G53830.1; AT1G53830.1; AT1G53830.
DR GeneID; 841820; -.
DR Gramene; AT1G53830.1; AT1G53830.1; AT1G53830.
DR KEGG; ath:AT1G53830; -.
DR Araport; AT1G53830; -.
DR TAIR; locus:2197056; AT1G53830.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; Q42534; -.
DR OMA; RPEGWHE; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q42534; -.
DR BioCyc; ARA:AT1G53830-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q42534; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42534; baseline and differential.
DR Genevisible; Q42534; AT.
DR GO; GO:0005576; C:extracellular region; ISS:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; ISS:TAIR.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:1990110; P:callus formation; IMP:TAIR.
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 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 TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 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..40
FT /evidence="ECO:0000255"
FT CHAIN 41..587
FT /note="Pectinesterase 2"
FT /id="PRO_0000023475"
FT ACT_SITE 404
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 425
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 403
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 418..438
FT /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="S -> F (in Ref. 4; AAC50023)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..241
FT /note="SSTFTNNNN -> FFNLHQQQQ (in Ref. 4; AAC50023)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..291
FT /note="TTVA -> DNGS (in Ref. 4; AAC50023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 64173 MW; FA8AB0F92D19A1E4 CRC64;
MAPIKEFISK FSDFKNNKKL ILSSAAIALL LLASIVGIAA TTTNQNKNQK ITTLSSTSHA
ILKSVCSSTL YPELCFSAVA ATGGKELTSQ KEVIEASLNL TTKAVKHNYF AVKKLIAKRK
GLTPREVTAL HDCLETIDET LDELHVAVED LHQYPKQKSL RKHADDLKTL ISSAITNQGT
CLDGFSYDDA DRKVRKALLK GQVHVEHMCS NALAMIKNMT ETDIANFELR DKSSTFTNNN
NRKLKEVTGD LDSDGWPKWL SVGDRRLLQG STIKADATVA DDGSGDFTTV AAAVAAAPEK
SNKRFVIHIK AGVYRENVEV TKKKTNIMFL GDGRGKTIIT GSRNVVDGST TFHSATVAAV
GERFLARDIT FQNTAGPSKH QAVALRVGSD FSAFYQCDMF AYQDTLYVHS NRQFFVKCHI
TGTVDFIFGN AAAVLQDCDI NARRPNSGQK NMVTAQGRSD PNQNTGIVIQ NCRIGGTSDL
LAVKGTFPTY LGRPWKEYSR TVIMQSDISD VIRPEGWHEW SGSFALDTLT YREYLNRGGG
AGTANRVKWK GYKVITSDTE AQPFTAGQFI GGGGWLASTG FPFSLSL
