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Protein

Pectinesterase PPME1

Gene

PPME1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts in the modification of cell walls via demethylesterification of cell wall pectin. Involved in the pollen tube growth and determination of pollen tube morphology.1 Publication

Catalytic activityi

Pectin + n H2O = n methanol + pectate.

Pathwayi: pectin degradation

This protein is involved in step 1 of the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Probable pectinesterase/pectinesterase inhibitor 7 (PME7), Probable pectinesterase 48 (PME48), Probable pectinesterase 49 (PME49), Probable pectinesterase 50 (PME50), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 19 (PME19), Probable pectinesterase/pectinesterase inhibitor 42 (PME42), Probable pectinesterase 15 (PME15), Probable pectinesterase/pectinesterase inhibitor 40 (PME40), Putative pectinesterase 14 (PME14), Pectinesterase (At3g10720), Probable pectinesterase 55 (PME55), Probable pectinesterase/pectinesterase inhibitor 23 (PME23), Pectinesterase 4 (PME4), Putative pectinesterase/pectinesterase inhibitor 22 (PME22), Probable pectinesterase/pectinesterase inhibitor 39 (PME39), Pectinesterase (At3g14310), Pectinesterase/pectinesterase inhibitor 18 (PME18), Putative pectinesterase/pectinesterase inhibitor 43 (PME43), Probable pectinesterase/pectinesterase inhibitor 34 (PME34), Pectinesterase 1 (PME1), Putative pectinesterase 63 (PME63), Putative pectinesterase 10 (PME10), Probable pectinesterase/pectinesterase inhibitor 64 (PME64), Pectinesterase (F14I3.7), Pectinesterase 2 (PME2), Probable pectinesterase 29 (PME29), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 21 (PME21), Putative pectinesterase/pectinesterase inhibitor 45 (PME45), Probable pectinesterase/pectinesterase inhibitor 12 (PME12), Probable pectinesterase/pectinesterase inhibitor 44 (PME44), Probable pectinesterase 8 (PME8), Pectinesterase, Pectinesterase/pectinesterase inhibitor 3 (PME3), Pectinesterase 31 (PME31), Probable pectinesterase/pectinesterase inhibitor 25 (PME25), Probable pectinesterase/pectinesterase inhibitor 51 (PME51), Probable pectinesterase/pectinesterase inhibitor 58 (PME58), Putative pectinesterase 57 (PME57), Pectinesterase (At3g62170), Probable pectinesterase/pectinesterase inhibitor 20 (PME20), Pectinesterase (T27B3.30), Probable pectinesterase/pectinesterase inhibitor 60 (PME60), Probable pectinesterase/pectinesterase inhibitor 59 (PME59), Pectinesterase QRT1 (QRT1), Putative pectinesterase 11 (PME11), Pectinesterase PPME1 (PPME1), Probable pectinesterase/pectinesterase inhibitor 32 (PME32), Probable pectinesterase/pectinesterase inhibitor 33 (PME33), Probable pectinesterase/pectinesterase inhibitor 36 (PME36), Probable pectinesterase/pectinesterase inhibitor 13 (PME13), Putative pectinesterase 52 (PME52), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 54 (PME54), Pectinesterase, Pectinesterase (At1g53840), Probable pectinesterase/pectinesterase inhibitor 16 (PME16), Pectinesterase 5 (PME5), Probable pectinesterase 30 (PME30), Probable pectinesterase/pectinesterase inhibitor VGDH2 (VGDH2), Putative pectinesterase/pectinesterase inhibitor 24 (PME24), Putative pectinesterase/pectinesterase inhibitor 26 (PME26), Probable pectinesterase/pectinesterase inhibitor 35 (PME35), Probable pectinesterase 68 (PME68), Pectinesterase, Probable pectinesterase 67 (PME67), Putative pectinesterase/pectinesterase inhibitor 38 (PME38), Probable pectinesterase 56 (PME56), Pectinesterase, Probable pectinesterase/pectinesterase inhibitor 47 (PME47), Putative pectinesterase/pectinesterase inhibitor 28 (PME28), Probable pectinesterase 53 (PME53), Probable pectinesterase/pectinesterase inhibitor 46 (PME46), Probable pectinesterase/pectinesterase inhibitor 17 (PME17), Probable pectinesterase/pectinesterase inhibitor 41 (PME41), Probable pectinesterase/pectinesterase inhibitor 61 (PME61), Probable pectinesterase 66 (PME66), Probable pectinesterase/pectinesterase inhibitor 6 (PME6)
  2. Pectate lyase (T26I12.20), Probable pectate lyase 7 (At3g01270), Probable pectate lyase 18 (At4g24780), Probable pectate lyase 16 (At4g22080), Putative pectate lyase 17 (At4g22090), Putative pectate lyase 14 (At4g13210), Pectate lyase (At3g55140), Probable pectate lyase 20 (At5g48900), Probable pectate lyase 6 (At2g02720), Pectate lyase (At1g14420), Pectate lyase (At3g01270), Pectate lyase (At2g02720), Probable pectate lyase 22 (At5g63180), Pectate lyase (T5E8_80), Pectate lyase (At3g01270), Pectate lyase (At3g55140), Putative pectate lyase 2 (At1g11920), Pectate lyase (At3g07010), Pectate lyase, Probable pectate lyase 8 (At3g07010), Probable pectate lyase 4 (At1g30350), Probable pectate lyase 19 (At5g15110), Pectate lyase (F11F8_12), Probable pectate lyase 13 (PMR6), Probable pectate lyase 3 (AT59), Probable pectate lyase 5 (At1g67750), Putative pectate lyase 21 (At5g55720), Pectate lyase (At4g13210), Probable pectate lyase 12 (At3g53190), Pectate lyase (At4g24780), Pectate lyase (At5g04310), Pectate lyase (At4g13710), Probable pectate lyase 15 (At4g13710), Pectate lyase (At3g53190), Pectate lyase (At3g01270), Putative pectate lyase 11 (At3g27400), Pectate lyase (At5g04310), Pectate lyase (At3g07010), Probable pectate lyase 9 (At3g24230), Probable pectate lyase 1 (At1g04680), Probable pectate lyase 10 (At3g24670)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway pectin degradation, which is itself part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin, the pathway pectin degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei174 – 1741SubstrateBy similarity
Sitei196 – 1961Transition state stabilizerBy similarity
Active sitei197 – 1971Proton donorBy similarity
Active sitei218 – 2181NucleophileBy similarity
Binding sitei275 – 2751SubstrateBy similarity
Binding sitei277 – 2771SubstrateBy similarity

GO - Molecular functioni

  • aspartyl esterase activity Source: UniProtKB-KW
  • pectinesterase activity Source: TAIR

GO - Biological processi

  • cell wall modification Source: InterPro
  • defense response to Gram-negative bacterium Source: TAIR
  • pectin catabolic process Source: UniProtKB-UniPathway
  • pollen tube growth Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciARA:AT1G69940-MONOMER.
BRENDAi3.1.1.11. 399.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectinesterase PPME1 (EC:3.1.1.11)
Short name:
AtPPME1
Short name:
PE PPME1
Alternative name(s):
Pectin methylesterase 9
Short name:
AtPME9
Pectin methylesterase PPME1
Protein POLLEN SPECIFIC PME 1
Gene namesi
Name:PPME1
Synonyms:ARATH9
Ordered Locus Names:At1g69940
ORF Names:T17F3.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G69940.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • extracellular region Source: UniProtKB-KW
  • Golgi apparatus Source: TAIR
  • plant-type cell wall Source: TAIR
  • pollen tube Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Endoplasmic reticulum, Golgi apparatus, Secreted

Pathology & Biotechi

Disruption phenotypei

After germination, the pollen tube is sunted, curved and has an irregular morphology. No effect on the morphology of ungerminated pollen grains, on the efficiency of pollen germination, fertilization or seed production.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 361338Pectinesterase PPME1PRO_0000371666Add
BLAST

Proteomic databases

PaxDbiQ84WM7.
PRIDEiQ84WM7.

Expressioni

Tissue specificityi

Expressed in mature pollen grains in the anthers and on the stigma. Found in pollen tubes within the style. Located at the tip and in the shank of the pollen tube.3 Publications

Gene expression databases

GenevisibleiQ84WM7. AT.

Interactioni

Subunit structurei

Interacts with PMEI2, and in vitro with PMEI1.1 Publication

Protein-protein interaction databases

STRINGi3702.AT1G69940.1.

Structurei

3D structure databases

ProteinModelPortaliQ84WM7.
SMRiQ84WM7. Positions 59-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pectinesterase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IKXJ. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ84WM7.
KOiK01051.
OMAiLNTETHV.
PhylomeDBiQ84WM7.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q84WM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYTNVSILL GLLMVFVTPM VFADDVTPIP EGKPQVAQWF NANVGPLAQR
60 70 80 90 100
KGLDPALVAA EAAPRIINVN PKGGEFKTLT DAIKSVPAGN TKRVIIKMAP
110 120 130 140 150
GEYKEKVTID RNKPFITLMG QPNAMPVITY DGTAAKYGTV DSASLIILSD
160 170 180 190 200
YFMAVNIVVK NTAPAPDGKT KGAQALSMRI SGNFAAFYNC KFYGFQDTIC
210 220 230 240 250
DDTGNHFFKD CYVEGTFDFI FGSGTSMYLG TQLHVVGDGI RVIAAHAGKS
260 270 280 290 300
AEEKSGYSFV HCKVTGTGGG IYLGRAWMSH PKVVYAYTEM TSVVNPTGWQ
310 320 330 340 350
ENKTPAHDKT VFYGEYKCSG PGSHKAKRVP FTQDIDDKEA NRFLSLGYIQ
360
GSKWLLPPPA L
Length:361
Mass (Da):39,142
Last modified:June 1, 2003 - v1
Checksum:iE71011347197DF4B
GO

Sequence cautioni

The sequence AAG52566.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010675 Genomic DNA. Translation: AAG52566.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35001.1.
BT002992 mRNA. Translation: AAO22801.1.
PIRiH96721.
RefSeqiNP_177152.2. NM_105663.4.
UniGeneiAt.20152.
At.48355.

Genome annotation databases

EnsemblPlantsiAT1G69940.1; AT1G69940.1; AT1G69940.
GeneIDi843331.
GrameneiAT1G69940.1; AT1G69940.1; AT1G69940.
KEGGiath:AT1G69940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010675 Genomic DNA. Translation: AAG52566.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE35001.1.
BT002992 mRNA. Translation: AAO22801.1.
PIRiH96721.
RefSeqiNP_177152.2. NM_105663.4.
UniGeneiAt.20152.
At.48355.

3D structure databases

ProteinModelPortaliQ84WM7.
SMRiQ84WM7. Positions 59-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G69940.1.

Proteomic databases

PaxDbiQ84WM7.
PRIDEiQ84WM7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G69940.1; AT1G69940.1; AT1G69940.
GeneIDi843331.
GrameneiAT1G69940.1; AT1G69940.1; AT1G69940.
KEGGiath:AT1G69940.

Organism-specific databases

TAIRiAT1G69940.

Phylogenomic databases

eggNOGiENOG410IKXJ. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ84WM7.
KOiK01051.
OMAiLNTETHV.
PhylomeDBiQ84WM7.

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BioCyciARA:AT1G69940-MONOMER.
BRENDAi3.1.1.11. 399.

Miscellaneous databases

PROiQ84WM7.

Gene expression databases

GenevisibleiQ84WM7. AT.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., 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.J., 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.Y., 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., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Pectin methylesterases: sequence-structural features and phylogenetic relationships."
    Markovic O., Janecek S.
    Carbohydr. Res. 339:2281-2295(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  5. "Pollen-specific pectin methylesterase involved in pollen tube growth."
    Tian G.-W., Chen M.-H., Zaltsman A., Citovsky V.
    Dev. Biol. 294:83-91(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  6. "Comprehensive expression profiling of the pectin methylesterase gene family during silique development in Arabidopsis thaliana."
    Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F., Guerineau F., Pelloux J.
    Planta 224:782-791(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Elaborate spatial patterning of cell-wall PME and PMEI at the pollen tube tip involves PMEI endocytosis, and reflects the distribution of esterified and de-esterified pectins."
    Roeckel N., Wolf S., Kost B., Rausch T., Greiner S.
    Plant J. 53:133-143(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PMEI1 AND PMEI2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPPME1_ARATH
AccessioniPrimary (citable) accession number: Q84WM7
Secondary accession number(s): Q9CAS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 2003
Last modified: February 17, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The pectin methylesterase activity is inhibited by PMEI2.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.