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Protein

Probable pectinesterase 53

Gene

PME53

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Acts in the modification of cell walls via demethylesterification of cell wall pectin.By similarity

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), Putative pectinesterase 14 (PME14), Probable pectinesterase/pectinesterase inhibitor 40 (PME40), Pectinesterase (At3g10720), Probable pectinesterase 55 (PME55), Probable pectinesterase/pectinesterase inhibitor 23 (PME23), Pectinesterase 4 (PME4), Probable pectinesterase/pectinesterase inhibitor 39 (PME39), Putative pectinesterase/pectinesterase inhibitor 22 (PME22), 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 8 (PME8), Probable pectinesterase/pectinesterase inhibitor 44 (PME44), 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), Pectinesterase QRT1 (QRT1), Probable pectinesterase/pectinesterase inhibitor 59 (PME59), 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), Pectinesterase 5 (PME5), Probable pectinesterase/pectinesterase inhibitor 16 (PME16), 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 sitei166 – 1661SubstrateBy similarity
Binding sitei201 – 2011SubstrateBy similarity
Sitei223 – 2231Transition state stabilizerBy similarity
Active sitei224 – 2241Proton donorPROSITE-ProRule annotation
Active sitei245 – 2451NucleophilePROSITE-ProRule annotation
Binding sitei301 – 3011SubstrateBy similarity
Binding sitei303 – 3031SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciARA:AT5G19730-MONOMER.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable pectinesterase 53 (EC:3.1.1.11)
Short name:
PE 53
Alternative name(s):
Pectin methylesterase 53
Short name:
AtPME53
Gene namesi
Name:PME53
Synonyms:ARATH53
Ordered Locus Names:At5g19730
ORF Names:T29J13.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G19730.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • cytoplasm Source: TAIR
  • extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 383355Probable pectinesterase 53PRO_0000371701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8VYZ3.
PRIDEiQ8VYZ3.

Expressioni

Tissue specificityi

Expressed in siliques.1 Publication

Developmental stagei

Expressed during late developmental phases of siliques.1 Publication

Gene expression databases

GenevisibleiQ8VYZ3. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G19730.1.

Structurei

3D structure databases

ProteinModelPortaliQ8VYZ3.
SMRiQ8VYZ3. Positions 94-382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pectinesterase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHQT. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ8VYZ3.
KOiK01051.
OMAiDPSREMT.
PhylomeDBiQ8VYZ3.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8VYZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKLNSTQAP NLFLLLLVIL LCSTQTQCHT KGLRLRPRNQ KNMNTTSDRT
60 70 80 90 100
QNPEDEFMKW VRFVGSLKHS VFKAAKNKLF PSYTLTVHKK SNKGDFTKIQ
110 120 130 140 150
DAIDSLPLIN FVRVVIKVHA GVYKEKVSIP PLKAFITIEG EGAEKTTVEW
160 170 180 190 200
GDTAQTPDSK GNPMGTYNSA SFAVNSPFFV AKNITFRNTT PVPLPGAVGK
210 220 230 240 250
QAVALRVSAD NAAFFGCRML GAQDTLYDHL GRHYYKDCYI EGSVDFIFGN
260 270 280 290 300
ALSLYEGCHV HAIADKLGAV TAQGRSSVLE DTGFSFVKCK VTGTGVLYLG
310 320 330 340 350
RAWGPFSRVV FAYTYMDNII LPRGWYNWGD PSREMTVFYG QYKCTGAGAN
360 370 380
YGGRVAWARE LTDEEAKPFL SLTFIDGSEW IKL
Length:383
Mass (Da):42,541
Last modified:March 1, 2002 - v1
Checksum:i3BA67E80D5301F21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296838 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92743.1.
AY065431 mRNA. Translation: AAL38872.1.
AY096559 mRNA. Translation: AAM20209.1.
RefSeqiNP_197474.1. NM_121978.3.
UniGeneiAt.28487.

Genome annotation databases

EnsemblPlantsiAT5G19730.1; AT5G19730.1; AT5G19730.
GeneIDi832093.
GrameneiAT5G19730.1; AT5G19730.1; AT5G19730.
KEGGiath:AT5G19730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296838 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92743.1.
AY065431 mRNA. Translation: AAL38872.1.
AY096559 mRNA. Translation: AAM20209.1.
RefSeqiNP_197474.1. NM_121978.3.
UniGeneiAt.28487.

3D structure databases

ProteinModelPortaliQ8VYZ3.
SMRiQ8VYZ3. Positions 94-382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G19730.1.

Proteomic databases

PaxDbiQ8VYZ3.
PRIDEiQ8VYZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G19730.1; AT5G19730.1; AT5G19730.
GeneIDi832093.
GrameneiAT5G19730.1; AT5G19730.1; AT5G19730.
KEGGiath:AT5G19730.

Organism-specific databases

TAIRiAT5G19730.

Phylogenomic databases

eggNOGiENOG410IHQT. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ8VYZ3.
KOiK01051.
OMAiDPSREMT.
PhylomeDBiQ8VYZ3.

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BioCyciARA:AT5G19730-MONOMER.

Miscellaneous databases

PROiQ8VYZ3.

Gene expression databases

GenevisibleiQ8VYZ3. AT.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR033131. Pectinesterase_Asp_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
PfamiPF01095. Pectinesterase. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(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. "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, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPME53_ARATH
AccessioniPrimary (citable) accession number: Q8VYZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2002
Last modified: March 16, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.