PME62_ARATH
ID PME62_ARATH Reviewed; 380 AA.
AC Q9FM79;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Pectinesterase QRT1 {ECO:0000303|PubMed:16980565};
DE Short=PE QRT1 {ECO:0000303|PubMed:16980565};
DE EC=3.1.1.11 {ECO:0000269|PubMed:16980565, ECO:0000269|PubMed:9744097};
DE AltName: Full=Pectin methylesterase 62 {ECO:0000303|PubMed:15337457};
DE Short=AtPME62 {ECO:0000303|PubMed:15337457};
DE AltName: Full=Pectin methylesterase QRT1 {ECO:0000303|PubMed:16980565};
DE AltName: Full=Protein QUARTET 1 {ECO:0000303|PubMed:16980565};
DE Short=AtQRT1 {ECO:0000303|PubMed:16980565};
DE Flags: Precursor;
GN Name=QRT1 {ECO:0000303|PubMed:16980565};
GN Synonyms=ARATH62 {ECO:0000303|PubMed:15337457};
GN OrderedLocusNames=At5g55590 {ECO:0000312|Araport:AT5G55590};
GN ORFNames=MDF20.3 {ECO:0000312|EMBL:BAB09226.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16980565; DOI=10.1104/pp.106.085274;
RA Francis K.E., Lam S.Y., Copenhaver G.P.;
RT "Separation of Arabidopsis pollen tetrads is regulated by QUARTET1, a
RT pectin methylesterase gene.";
RL Plant Physiol. 142:1004-1013(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=8197459; DOI=10.1126/science.8197459;
RA Preuss D., Rhee S.Y., Davis R.W.;
RT "Tetrad analysis possible in Arabidopsis with mutation of the QUARTET (QRT)
RT genes.";
RL Science 264:1458-1460(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9744097; DOI=10.1046/j.1365-313x.1998.00183.x;
RA Rhee S.Y., Somerville C.R.;
RT "Tetrad pollen formation in quartet mutants of Arabidopsis thaliana is
RT associated with persistence of pectic polysaccharides of the pollen mother
RT cell wall.";
RL Plant J. 15:79-88(1998).
RN [6]
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 [7]
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: Pectinesterase required for cell type-specific pectin
CC degradation to separate microspores. {ECO:0000269|PubMed:16980565,
CC ECO:0000269|PubMed:8197459, ECO:0000269|PubMed:9744097}.
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:0000269|PubMed:16980565, ECO:0000269|PubMed:9744097};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000269|PubMed:16980565,
CC ECO:0000269|PubMed:9744097}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds, siliques, developing
CC guard cells, floral nectares, at the stigmatic surface, in the
CC hypocotyl-root transition zone and the area of lateral root emergence.
CC Not expressed in mature leaves. {ECO:0000269|PubMed:16622707,
CC ECO:0000269|PubMed:16980565}.
CC -!- DEVELOPMENTAL STAGE: Expressed in anther tissues shortly after meiosis
CC is completed and during the late developmental phases of siliques.
CC {ECO:0000269|PubMed:16622707, ECO:0000269|PubMed:16980565}.
CC -!- DISRUPTION PHENOTYPE: The mature pollen grains are arranged in a
CC tetrad. {ECO:0000269|PubMed:16980565}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; DQ979876; ABI97858.1; -; mRNA.
DR EMBL; AB009050; BAB09226.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96653.1; -; Genomic_DNA.
DR RefSeq; NP_200370.1; NM_124941.3.
DR AlphaFoldDB; Q9FM79; -.
DR SMR; Q9FM79; -.
DR STRING; 3702.AT5G55590.1; -.
DR PaxDb; Q9FM79; -.
DR PRIDE; Q9FM79; -.
DR EnsemblPlants; AT5G55590.1; AT5G55590.1; AT5G55590.
DR GeneID; 835653; -.
DR Gramene; AT5G55590.1; AT5G55590.1; AT5G55590.
DR KEGG; ath:AT5G55590; -.
DR Araport; AT5G55590; -.
DR TAIR; locus:2162102; AT5G55590.
DR eggNOG; ENOG502QS8M; Eukaryota.
DR HOGENOM; CLU_012243_3_3_1; -.
DR InParanoid; Q9FM79; -.
DR OMA; TRDEVKP; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9FM79; -.
DR BioCyc; ARA:AT5G55590-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9FM79; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM79; baseline and differential.
DR Genevisible; Q9FM79; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IDA:TAIR.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IMP: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 Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..380
FT /note="Pectinesterase QRT1"
FT /id="PRO_0000369432"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT SITE 220
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 235..255
FT /evidence="ECO:0000250|UniProtKB:P0C1A9"
SQ SEQUENCE 380 AA; 42475 MW; E5F90B49EB73EF64 CRC64;
MKVEAFIPAV LLLCFGVMLC LKSSCALQIG NNNELKNYIS WEDLRVVEDG RIERSFSIKE
NSNWVTTNAN ANANATNVRR VIVVDKNGGG DSVTVQGAVD MVPDSNSQRV KIFILPGIYR
EKVIVPKSKP YISFIGNESY AGDTVISWSD KASDLGCDGK ELGTYRTASV SIESDFFCAT
AITFENTVVA EAGEQGRQAV ALRIIGDKAV FYRVRVLGSQ DTLFDDNGSH YFYQCYIQGN
VDFIFGNAKS LYQDCDIHST AKRYGAIAAH HRDSETEDTG FSFVNCDISG TGQIYLGRAW
GNYSRTVYSN CFIADIITPV GWSDWKHPER QRKVMFGEYN CRGRGAERGG RVPWSKTLTR
DEVKPFLGRE FIYGDQWLRL
