PPME1_ARATH
ID PPME1_ARATH Reviewed; 361 AA.
AC Q84WM7; Q9CAS7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Pectinesterase PPME1;
DE Short=AtPPME1 {ECO:0000303|PubMed:16564517};
DE Short=PE PPME1;
DE EC=3.1.1.11 {ECO:0000305|PubMed:16564517};
DE AltName: Full=Pectin methylesterase 9;
DE Short=AtPME9;
DE AltName: Full=Pectin methylesterase PPME1;
DE AltName: Full=Protein POLLEN SPECIFIC PME 1;
DE Flags: Precursor;
GN Name=PPME1; Synonyms=ARATH9; OrderedLocusNames=At1g69940; ORFNames=T17F3.3;
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 IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16564517; DOI=10.1016/j.ydbio.2006.02.026;
RA Tian G.-W., Chen M.-H., Zaltsman A., Citovsky V.;
RT "Pollen-specific pectin methylesterase involved in pollen tube growth.";
RL Dev. Biol. 294:83-91(2006).
RN [6]
RP TISSUE SPECIFICITY.
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).
RN [7]
RP INTERACTION WITH PMEI1 AND PMEI2, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17971035; DOI=10.1111/j.1365-313x.2007.03325.x;
RA Roeckel N., Wolf S., Kost B., Rausch T., Greiner S.;
RT "Elaborate spatial patterning of cell-wall PME and PMEI at the pollen tube
RT tip involves PMEI endocytosis, and reflects the distribution of esterified
RT and de-esterified pectins.";
RL Plant J. 53:133-143(2008).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. Involved in the pollen tube
CC growth and determination of pollen tube morphology.
CC {ECO:0000269|PubMed:16564517}.
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 Evidence={ECO:0000305|PubMed:16564517};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22381;
CC Evidence={ECO:0000305|PubMed:16564517};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBUNIT: Interacts with PMEI2, and in vitro with PMEI1.
CC {ECO:0000269|PubMed:17971035}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus. Secreted,
CC cell wall.
CC -!- TISSUE SPECIFICITY: Expressed in mature pollen grains in the anthers
CC and on the stigma. Found in pollen tubes within the style. Located at
CC the tip and in the shank of the pollen tube.
CC {ECO:0000269|PubMed:16564517, ECO:0000269|PubMed:16622707,
CC ECO:0000269|PubMed:17971035}.
CC -!- DISRUPTION PHENOTYPE: After germination, the pollen tube is sunted,
CC curved and has an irregular morphology. No effect on the morphology of
CC ungerminated pollen grains, on the efficiency of pollen germination,
CC fertilization or seed production. {ECO:0000269|PubMed:16564517}.
CC -!- MISCELLANEOUS: The pectin methylesterase activity is inhibited by
CC PMEI2.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52566.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010675; AAG52566.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35001.1; -; Genomic_DNA.
DR EMBL; BT002992; AAO22801.1; -; mRNA.
DR PIR; H96721; H96721.
DR RefSeq; NP_177152.2; NM_105663.5.
DR AlphaFoldDB; Q84WM7; -.
DR SMR; Q84WM7; -.
DR STRING; 3702.AT1G69940.1; -.
DR PaxDb; Q84WM7; -.
DR PRIDE; Q84WM7; -.
DR ProteomicsDB; 236584; -.
DR EnsemblPlants; AT1G69940.1; AT1G69940.1; AT1G69940.
DR GeneID; 843331; -.
DR Gramene; AT1G69940.1; AT1G69940.1; AT1G69940.
DR KEGG; ath:AT1G69940; -.
DR Araport; AT1G69940; -.
DR TAIR; locus:2196805; AT1G69940.
DR eggNOG; ENOG502R3C8; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q84WM7; -.
DR OMA; FSFVHCM; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q84WM7; -.
DR BioCyc; ARA:AT1G69940-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q84WM7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84WM7; baseline and differential.
DR Genevisible; Q84WM7; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; NAS:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; NAS:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0030599; F:pectinesterase activity; IMP:TAIR.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IDA:TAIR.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..361
FT /note="Pectinesterase PPME1"
FT /id="PRO_0000371666"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 361 AA; 39142 MW; E71011347197DF4B CRC64;
MGYTNVSILL GLLMVFVTPM VFADDVTPIP EGKPQVAQWF NANVGPLAQR KGLDPALVAA
EAAPRIINVN PKGGEFKTLT DAIKSVPAGN TKRVIIKMAP GEYKEKVTID RNKPFITLMG
QPNAMPVITY DGTAAKYGTV DSASLIILSD YFMAVNIVVK NTAPAPDGKT KGAQALSMRI
SGNFAAFYNC KFYGFQDTIC DDTGNHFFKD CYVEGTFDFI FGSGTSMYLG TQLHVVGDGI
RVIAAHAGKS AEEKSGYSFV HCKVTGTGGG IYLGRAWMSH PKVVYAYTEM TSVVNPTGWQ
ENKTPAHDKT VFYGEYKCSG PGSHKAKRVP FTQDIDDKEA NRFLSLGYIQ GSKWLLPPPA
L
