PME26_ARATH
ID PME26_ARATH Reviewed; 968 AA.
AC Q9LUL8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative pectinesterase/pectinesterase inhibitor 26;
DE AltName: Full=AtPMEpcrC;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 26;
DE AltName: Full=Pectin methylesterase inhibitor 26;
DE Includes:
DE RecName: Full=Pectinesterase 26;
DE Short=PE 26;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 26;
DE Short=AtPME26;
GN Name=PME26; Synonyms=ARATH26; OrderedLocusNames=At3g14300;
GN ORFNames=MLN21.8;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 TISSUE SPECIFICITY.
RX PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA Micheli F., Holliger C., Goldberg R., Richard L.;
RT "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT member of a gene family comprising at least 12 genes in Arabidopsis
RT thaliana.";
RL Gene 220:13-20(1998).
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).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers. {ECO:0000269|PubMed:9767082}.
CC -!- MISCELLANEOUS: The PMEI regions may act as autoinhibitory domains and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
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DR EMBL; AB022220; BAB01036.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75499.1; -; Genomic_DNA.
DR RefSeq; NP_188047.1; NM_112288.2.
DR AlphaFoldDB; Q9LUL8; -.
DR SMR; Q9LUL8; -.
DR STRING; 3702.AT3G14300.1; -.
DR PaxDb; Q9LUL8; -.
DR PRIDE; Q9LUL8; -.
DR ProteomicsDB; 234779; -.
DR EnsemblPlants; AT3G14300.1; AT3G14300.1; AT3G14300.
DR GeneID; 820650; -.
DR Gramene; AT3G14300.1; AT3G14300.1; AT3G14300.
DR KEGG; ath:AT3G14300; -.
DR Araport; AT3G14300; -.
DR TAIR; locus:2091070; AT3G14300.
DR eggNOG; ENOG502RA2Q; Eukaryota.
DR HOGENOM; CLU_306163_0_0_1; -.
DR InParanoid; Q9LUL8; -.
DR OMA; DEISHTN; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q9LUL8; -.
DR BioCyc; ARA:AT3G14300-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q9LUL8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUL8; differential.
DR Genevisible; Q9LUL8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; ISS:TAIR.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 3.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 3.
DR SMART; SM00856; PMEI; 3.
DR SUPFAM; SSF101148; SSF101148; 3.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 3.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..968
FT /note="Putative pectinesterase/pectinesterase inhibitor 26"
FT /id="PRO_0000370189"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 71..230
FT /note="Pectinesterase inhibitor 26 A"
FT REGION 265..430
FT /note="Pectinesterase inhibitor 26 B"
FT REGION 453..614
FT /note="Pectinesterase inhibitor 26 C"
FT REGION 660..954
FT /note="Pectinesterase 26"
FT ACT_SITE 788
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 809
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 735
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 765
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 872
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 874
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 787
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 802..822
FT /evidence="ECO:0000250"
SQ SEQUENCE 968 AA; 105628 MW; 96DB0EAFAFA43898 CRC64;
MDTVKSINKG YGKVDETQDL ALKRKTRKRL YQIGISVAVL VAIIISSTVT IAIHSRKGNS
PHPTPSSVPE LTPAASLKTV CSVTNYPVSC FSSISKLPLS NTTDPEVIFR LSLQVVIDEL
NSIVELPKKL AEETDDEGLK SALSVCEHLL DLAIDRVNET VSAMEVVDGK KILNAATIDD
LLTWLSAAVT YHGTCLDALD EISHTNSAIP LKLKSGMVNS TEFTSNSLAI VAKILSTISD
FGIPIHGRRL LNSSPHATPI SVPKLTPAAS LRNVCSVTRY PASCVSSISK LPSSNTTDPE
ALFRLSLQVV INELNSIAGL PKKLAEETDD ERLKSSLSVC GDVFNDAIDI VNDTISTMEE
VGDGKKILKS STIDEIQTWL SAAVTDHDTC LDALDELSQN KTEYANSPIS LKLKSAMVNS
RKFTSNSLAI IAKFPIHERH GVQSPRLRKS PHPTPSSVLR TVCNVTNYPA SCISSISKLP
LSKTTTDPKV LFRLSLQVTF DELNSIVGLP KKLAEETNDE GLKSALSVCA DVFDLAVDSV
NDTISSLDEV ISGGKKNLNS STIGDLITWL SSAVTDIGTC GDTLDEDNYN SPIPQKLKSA
MVNSTEFTSN SLAIVAQVLK KPSKSRIPVQ GRRLLNSNSF PNWVRPGVRR LLQAKNLTPH
VTVAADGSGD VRTVNEAVWR VPKKGKTMFV IYVKAGTYVE NVLMKKDKWN VFIYGDGRDK
TIISGSTNMV DGVRTFNTST FATEGKGFMM KDMGIINTAG PEKHQAVAFR SDSDRSVYYR
CSFDGYQDTL YTHSNRQYYR NCDVTGTVDF IFGAGTVVFQ GCSIRPRQPL PNQFNTITAE
GTQEANQNTG ISIHQCTISP NGNVTATTYL GRPWKLFSKT VIMQSVIGSF VNPAGWIAWN
STYDPPPRTI FYREYKNSGP GSDLSKRVKW AGYKPISSDD EAARFTVKYF LRGDDNWIPK
AVMGMPPL
