PME64_ARATH
ID PME64_ARATH Reviewed; 602 AA.
AC Q8L7Q7; Q9FLF6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 64;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 64;
DE AltName: Full=Pectin methylesterase inhibitor 64;
DE Includes:
DE RecName: Full=Pectinesterase 64;
DE Short=PE 64;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 64;
DE Short=AtPME64;
GN Name=PME64; Synonyms=ARATH64; OrderedLocusNames=At5g64640;
GN ORFNames=MUB3.16;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-602.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [5]
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: 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 siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
CC siliques. {ECO:0000269|PubMed:16622707}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM91523.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB010076; BAB11431.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97931.1; -; Genomic_DNA.
DR EMBL; AY128320; AAM91523.1; ALT_INIT; mRNA.
DR RefSeq; NP_568991.2; NM_125860.5.
DR AlphaFoldDB; Q8L7Q7; -.
DR SMR; Q8L7Q7; -.
DR STRING; 3702.AT5G64640.1; -.
DR PaxDb; Q8L7Q7; -.
DR PRIDE; Q8L7Q7; -.
DR ProteomicsDB; 226149; -.
DR EnsemblPlants; AT5G64640.1; AT5G64640.1; AT5G64640.
DR GeneID; 836585; -.
DR Gramene; AT5G64640.1; AT5G64640.1; AT5G64640.
DR KEGG; ath:AT5G64640; -.
DR Araport; AT5G64640; -.
DR TAIR; locus:2174794; AT5G64640.
DR eggNOG; ENOG502QW0X; Eukaryota.
DR HOGENOM; CLU_012243_9_3_1; -.
DR InParanoid; Q8L7Q7; -.
DR OMA; WIRPATE; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q8L7Q7; -.
DR BioCyc; ARA:AT5G64640-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q8L7Q7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7Q7; baseline and differential.
DR Genevisible; Q8L7Q7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.140.40; -; 1.
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; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..602
FT /note="Probable pectinesterase/pectinesterase inhibitor 64"
FT /id="PRO_0000371709"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 62..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..237
FT /note="Pectinesterase inhibitor 64"
FT REGION 288..595
FT /note="Pectinesterase 64"
FT COMPBIAS 74..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 441
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 518
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 419
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 434..454
FT /evidence="ECO:0000250"
SQ SEQUENCE 602 AA; 65478 MW; 1667501044317054 CRC64;
MDSPTLPHSI SASSSTPFAS AAVKPHRNKL LSRNGILIII AASCILLLLI SLLIYATVSK
SSRNHHNPSH QTPTSDDHPP PETPPSPPPI AQIRLACNAT RFPDHCVASL SKPGQVPPDP
KPVQIIHSAI SVSYENLKSG QSKIQSILDS SAGNRNRTNI ATICLEILSY SQHRTESTDI
AVTSGDIKDA RAWMSAALAY QFDCWSGLKT VNDTKQVVDT ITFFEGLVNL TGNALSMMLS
FDSFGDDVVS WIRPATERDG FWEKAGPSLG SGTGTEASLG FPSGLTEDVT VCKNGGKDCK
YKTVQEAVDS APDTNRTVKF VIRIREGVYE ETVRVPFEKK NVVFIGDGMG KTVITGSLNV
GQPGMTTFES ATVGVLGDGF MARDLTIENT AGADAHQAVA FRSDSDFSVL ENCEFLGNQD
TLYAHSLRQF YKQCRIQGNV DFIFGNSAAV FQDCDILIAS KHSKLEQGGA NNAITAHGRI
DASQSTGFVF LNCSINGTEE YMKEFQANPE GHKNFLGRPW KEFSRTVFVN CNLESLISPD
GWMPWNGDFA LKTLYYGEYK NTGPGSVRSS RVPWSSEIPE KHVDVYSVAN FIQADEWAST
TA
