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Probable pectinesterase/pectinesterase inhibitor 64 [Includes: Pectinesterase inhibitor 64 (Pectin methylesterase inhibitor 64); Pectinesterase 64 (PE 64) (EC 3.1.1.11) (Pectin methylesterase 64) (AtPME64)]

 PME64_ARATH             Reviewed;         602 AA.
Q8L7Q7; Q9FLF6;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 81.
RecName: Full=Probable pectinesterase/pectinesterase inhibitor 64;
Includes:
RecName: Full=Pectinesterase inhibitor 64;
AltName: Full=Pectin methylesterase inhibitor 64;
Includes:
RecName: Full=Pectinesterase 64;
Short=PE 64;
EC=3.1.1.11;
AltName: Full=Pectin methylesterase 64;
Short=AtPME64;
Name=PME64; Synonyms=ARATH64; OrderedLocusNames=At5g64640;
ORFNames=MUB3.16;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"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.";
DNA Res. 5:41-54(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-602.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
Markovic O., Janecek S.;
"Pectin methylesterases: sequence-structural features and phylogenetic
relationships.";
Carbohydr. Res. 339:2281-2295(2004).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
Guerineau F., Pelloux J.;
"Comprehensive expression profiling of the pectin methylesterase gene
family during silique development in Arabidopsis thaliana.";
Planta 224:782-791(2006).
-!- FUNCTION: Acts in the modification of cell walls via
demethylesterification of cell wall pectin. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Pectin + n H(2)O = n methanol + pectate.
-!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-
D-gluconate from pectin: step 1/5.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in siliques.
{ECO:0000269|PubMed:16622707}.
-!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
siliques. {ECO:0000269|PubMed:16622707}.
-!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain
and prevent untimely PME activity during transport.
-!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
pectinesterase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM91523.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB010076; BAB11431.1; -; Genomic_DNA.
EMBL; CP002688; AED97931.1; -; Genomic_DNA.
EMBL; AY128320; AAM91523.1; ALT_INIT; mRNA.
RefSeq; NP_568991.2; NM_125860.5.
UniGene; At.28947; -.
UniGene; At.69346; -.
ProteinModelPortal; Q8L7Q7; -.
SMR; Q8L7Q7; -.
STRING; 3702.AT5G64640.1; -.
PaxDb; Q8L7Q7; -.
PRIDE; Q8L7Q7; -.
EnsemblPlants; AT5G64640.1; AT5G64640.1; AT5G64640.
GeneID; 836585; -.
Gramene; AT5G64640.1; AT5G64640.1; AT5G64640.
KEGG; ath:AT5G64640; -.
Araport; AT5G64640; -.
TAIR; locus:2174794; AT5G64640.
eggNOG; ENOG410IFZX; Eukaryota.
eggNOG; COG4677; LUCA.
HOGENOM; HOG000217409; -.
InParanoid; Q8L7Q7; -.
OMA; YQYDCSH; -.
OrthoDB; EOG0936077N; -.
PhylomeDB; Q8L7Q7; -.
BioCyc; ARA:AT5G64640-MONOMER; -.
BRENDA; 3.1.1.11; 399.
UniPathway; UPA00545; UER00823.
PRO; PR:Q8L7Q7; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q8L7Q7; AT.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0005618; C:cell wall; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
GO; GO:0042545; P:cell wall modification; IEA:InterPro.
GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.20.140.40; -; 1.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR035513; Invertase/methylesterase_inhib.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR000070; Pectinesterase_cat.
InterPro; IPR006501; Pectinesterase_inhib_dom.
Pfam; PF01095; Pectinesterase; 1.
Pfam; PF04043; PMEI; 1.
SMART; SM00856; PMEI; 1.
SUPFAM; SSF101148; SSF101148; 1.
SUPFAM; SSF51126; SSF51126; 1.
TIGRFAMs; TIGR01614; PME_inhib; 1.
2: Evidence at transcript level;
Aspartyl esterase; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Membrane; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 602 Probable pectinesterase/pectinesterase
inhibitor 64.
/FTId=PRO_0000371709.
TRANSMEM 36 56 Helical. {ECO:0000255}.
REGION 87 237 Pectinesterase inhibitor 64.
REGION 288 595 Pectinesterase 64.
COMPBIAS 68 122 Pro-rich.
ACT_SITE 420 420 Proton donor; for pectinesterase
activity. {ECO:0000250}.
ACT_SITE 441 441 Nucleophile; for pectinesterase activity.
{ECO:0000250}.
BINDING 367 367 Substrate; for pectinesterase activity.
{ECO:0000250}.
BINDING 397 397 Substrate; for pectinesterase activity.
{ECO:0000250}.
BINDING 518 518 Substrate; for pectinesterase activity.
{ECO:0000250}.
BINDING 520 520 Substrate; for pectinesterase activity.
{ECO:0000250}.
SITE 419 419 Transition state stabilizer.
{ECO:0000250}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 434 454 {ECO:0000250}.
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


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