PME56_ARATH
ID PME56_ARATH Reviewed; 288 AA.
AC Q4PT34; Q9LPZ8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable pectinesterase 56;
DE Short=PE 56;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 56;
DE Short=AtPME56;
DE Flags: Precursor;
GN Name=PME56; Synonyms=ARATH56; OrderedLocusNames=At1g11370;
GN ORFNames=T23J18.3;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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: Secreted, cell wall {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16649.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011661; AAF16649.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28727.1; -; Genomic_DNA.
DR EMBL; DQ056452; AAY78609.1; -; mRNA.
DR PIR; F86247; F86247.
DR RefSeq; NP_172604.1; NM_101010.2.
DR AlphaFoldDB; Q4PT34; -.
DR SMR; Q4PT34; -.
DR STRING; 3702.AT1G11370.1; -.
DR PaxDb; Q4PT34; -.
DR PRIDE; Q4PT34; -.
DR EnsemblPlants; AT1G11370.1; AT1G11370.1; AT1G11370.
DR GeneID; 837679; -.
DR Gramene; AT1G11370.1; AT1G11370.1; AT1G11370.
DR KEGG; ath:AT1G11370; -.
DR Araport; AT1G11370; -.
DR TAIR; locus:2200156; AT1G11370.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_4_0_1; -.
DR InParanoid; Q4PT34; -.
DR OMA; WIEFITR; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q4PT34; -.
DR BioCyc; ARA:AT1G11370-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q4PT34; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q4PT34; baseline and differential.
DR Genevisible; Q4PT34; 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: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:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
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 Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..288
FT /note="Probable pectinesterase 56"
FT /id="PRO_0000371704"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 288 AA; 31400 MW; 0643EEF1B0EE2549 CRC64;
MAMTSTMQLL VLSFLVIASL FLGATVAPPA SLISTPDQAL KDKADLIVAK DGSGNFTTVN
EAVAAAPENG VKPFVIYIKE GLYKEVIRIG KKKTNLTLVG DGRDLTVLSG DLNGVDGIKT
FDSATLAVDE SGFMAQDLCI RNTAGPEKRQ AVALRISTDM TIIYRCRIDA YQDTLYAYSG
RQFYRDCYIT GTVDFIFGRA AAVFQYCQIE ARKPGIGQTN ILTAQSREED TATSGFSFQK
CNISASSDLT PIKGTVKTFL GRPWRAFSRV VFMESFIDDV IDRAGWTP
