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Protein

Pectinesterase QRT1

Gene

QRT1

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

Functioni

Pectinesterase required for cell type-specific pectin degradation to separate microspores.3 Publications

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 sitei164 – 1641SubstrateBy similarity
Binding sitei198 – 1981SubstrateBy similarity
Sitei220 – 2201Transition state stabilizerBy similarity
Active sitei221 – 2211Proton donorBy similarity
Active sitei242 – 2421NucleophileBy similarity
Binding sitei298 – 2981SubstrateBy similarity
Binding sitei300 – 3001SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • cell wall modification Source: InterPro
  • pectin catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl esterase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciARA:AT5G55590-MONOMER.
UniPathwayiUPA00545; UER00823.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectinesterase QRT1 (EC:3.1.1.11)
Short name:
AtQRT1
Short name:
PE QRT1
Alternative name(s):
Pectin methylesterase 62
Short name:
AtPME62
Pectin methylesterase QRT1
Protein QUARTET 1
Gene namesi
Name:QRT1
Synonyms:ARATH62
Ordered Locus Names:At5g55590
ORF Names:MDF20.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G55590.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Disruption phenotypei

The mature pollen grains are arranged in a tetrad.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 380354Pectinesterase QRT1PRO_0000369432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence analysis
Disulfide bondi235 ↔ 255By similarity
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9FM79.
PRIDEiQ9FM79.

Expressioni

Tissue specificityi

Expressed in flower buds, siliques, developing guard cells, floral nectares, at the stigmatic surface, in the hypocotyl-root transition zone and the area of lateral root emergence. Not expressed in mature leaves.2 Publications

Developmental stagei

Expressed in anther tissues shortly after meiosis is completed and during the late developmental phases of siliques.2 Publications

Gene expression databases

GenevisibleiQ9FM79. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G55590.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FM79.
SMRiQ9FM79. Positions 82-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pectinesterase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGNA. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ9FM79.
KOiK01051.
OMAiHRDSETE.
PhylomeDBiQ9FM79.

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.

Q9FM79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVEAFIPAV LLLCFGVMLC LKSSCALQIG NNNELKNYIS WEDLRVVEDG
60 70 80 90 100
RIERSFSIKE NSNWVTTNAN ANANATNVRR VIVVDKNGGG DSVTVQGAVD
110 120 130 140 150
MVPDSNSQRV KIFILPGIYR EKVIVPKSKP YISFIGNESY AGDTVISWSD
160 170 180 190 200
KASDLGCDGK ELGTYRTASV SIESDFFCAT AITFENTVVA EAGEQGRQAV
210 220 230 240 250
ALRIIGDKAV FYRVRVLGSQ DTLFDDNGSH YFYQCYIQGN VDFIFGNAKS
260 270 280 290 300
LYQDCDIHST AKRYGAIAAH HRDSETEDTG FSFVNCDISG TGQIYLGRAW
310 320 330 340 350
GNYSRTVYSN CFIADIITPV GWSDWKHPER QRKVMFGEYN CRGRGAERGG
360 370 380
RVPWSKTLTR DEVKPFLGRE FIYGDQWLRL
Length:380
Mass (Da):42,475
Last modified:March 1, 2001 - v1
Checksum:iE5F90B49EB73EF64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ979876 mRNA. Translation: ABI97858.1.
AB009050 Genomic DNA. Translation: BAB09226.1.
CP002688 Genomic DNA. Translation: AED96653.1.
RefSeqiNP_200370.1. NM_124941.2.
UniGeneiAt.29433.
At.6552.

Genome annotation databases

EnsemblPlantsiAT5G55590.1; AT5G55590.1; AT5G55590.
GeneIDi835653.
GrameneiAT5G55590.1; AT5G55590.1; AT5G55590.
KEGGiath:AT5G55590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ979876 mRNA. Translation: ABI97858.1.
AB009050 Genomic DNA. Translation: BAB09226.1.
CP002688 Genomic DNA. Translation: AED96653.1.
RefSeqiNP_200370.1. NM_124941.2.
UniGeneiAt.29433.
At.6552.

3D structure databases

ProteinModelPortaliQ9FM79.
SMRiQ9FM79. Positions 82-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G55590.1.

Proteomic databases

PaxDbiQ9FM79.
PRIDEiQ9FM79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G55590.1; AT5G55590.1; AT5G55590.
GeneIDi835653.
GrameneiAT5G55590.1; AT5G55590.1; AT5G55590.
KEGGiath:AT5G55590.

Organism-specific databases

TAIRiAT5G55590.

Phylogenomic databases

eggNOGiENOG410IGNA. Eukaryota.
COG4677. LUCA.
HOGENOMiHOG000217409.
InParanoidiQ9FM79.
KOiK01051.
OMAiHRDSETE.
PhylomeDBiQ9FM79.

Enzyme and pathway databases

UniPathwayiUPA00545; UER00823.
BioCyciARA:AT5G55590-MONOMER.

Miscellaneous databases

PROiQ9FM79.

Gene expression databases

GenevisibleiQ9FM79. 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. "Separation of Arabidopsis pollen tetrads is regulated by QUARTET1, a pectin methylesterase gene."
    Francis K.E., Lam S.Y., Copenhaver G.P.
    Plant Physiol. 142:1004-1013(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Tetrad analysis possible in Arabidopsis with mutation of the QUARTET (QRT) genes."
    Preuss D., Rhee S.Y., Davis R.W.
    Science 264:1458-1460(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Tetrad pollen formation in quartet mutants of Arabidopsis thaliana is associated with persistence of pectic polysaccharides of the pollen mother cell wall."
    Rhee S.Y., Somerville C.R.
    Plant J. 15:79-88(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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.
  7. "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 nameiPME62_ARATH
AccessioniPrimary (citable) accession number: Q9FM79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 1, 2001
Last modified: February 17, 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.