ID A0A059BQ52_EUCGR Unreviewed; 286 AA.
AC A0A059BQ52;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pectinesterase {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
GN ORFNames=EUGRSUZ_F01581 {ECO:0000313|EMBL:KCW67860.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW67860.1};
RN [1] {ECO:0000313|EMBL:KCW67860.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW67860.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin.
CC {ECO:0000256|RuleBase:RU000589}.
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:0000256|ARBA:ARBA00001440,
CC ECO:0000256|RuleBase:RU000589};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184,
CC ECO:0000256|RuleBase:RU000589}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|RuleBase:RU000589}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; KK198758; KCW67860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059BQ52; -.
DR STRING; 71139.A0A059BQ52; -.
DR EnsemblPlants; KCW67860; KCW67860; EUGRSUZ_F01581.
DR Gramene; KCW67860; KCW67860; EUGRSUZ_F01581.
DR InParanoid; A0A059BQ52; -.
DR OMA; ENTFQRH; -.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF130; PECTINESTERASE 11-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Cell wall {ECO:0000256|RuleBase:RU000589};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU000589};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Secreted {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 26..286
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005102380"
FT DOMAIN 39..193
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT DOMAIN 200..261
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 286 AA; 31334 MW; DCD1677253B4A920 CRC64;
MRNQGQFILY FLLALLSACT NFSEAGNGTQ APNLARLILV DPSGKGNFRK IQDAIDAVPS
NNSELVFIRV EPGTYREKLV VPADKPFITL SGKKASSTIV TGDDSGDIFG SPTISVLASD
FVGRYLTIQN TYGSGAKAVV LRVSGDRVAF SACRITSHQD TLLDDVGRHY YSNCYIEGDV
DFIFGNAASL FQHRASPLEN TGFIFLGCPW GPYSRVVFAL SYMSSAVLPQ GWDDRGDSTK
QRTAYYGQYE CYGPGADTSK REVSPLLTMD MVDQQSWFKN APTIFN
//
