ID A0A059C525_EUCGR Unreviewed; 513 AA.
AC A0A059C525;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_E01468 {ECO:0000313|EMBL:KCW73025.1};
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:KCW73025.1};
RN [1] {ECO:0000313|EMBL:KCW73025.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW73025.1};
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 -!- 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|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 -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000256|ARBA:ARBA00007786}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000256|ARBA:ARBA00006027}.
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DR EMBL; KK198757; KCW73025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059C525; -.
DR STRING; 71139.A0A059C525; -.
DR EnsemblPlants; KCW73025; KCW73025; EUGRSUZ_E01468.
DR Gramene; KCW73025; KCW73025; EUGRSUZ_E01468.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR InParanoid; A0A059C525; -.
DR OMA; YENTVER; -.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd15798; PMEI-like_3; 1.
DR Gene3D; 1.20.140.40; Invertase/pectin methylesterase inhibitor family protein; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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 NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF149; PECTINESTERASE_PECTINESTERASE INHIBITOR 17-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 23..513
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005102376"
FT DOMAIN 24..168
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT NON_TER 513
FT /evidence="ECO:0000313|EMBL:KCW73025.1"
SQ SEQUENCE 513 AA; 56823 MW; 7BFBA94B94B2955F CRC64;
MGFHQKAITL LFLLLLLSQT ISSNSSSVVK SWCSKMPYPQ PCEHFLTRNP KQTPLKRRSH
FLRASMQVAL ESAQLAQTHT YSLGSGCHDE REKAAWADCL KLYEHTVHHL NRTINRRCTQ
DDMQTWLSAA LTNLQTCGTG FVELGISDNV LPLMSNNVSK LISNTLSANY VPYTTPNYTN
EFPTWVRLGD RKLLQSSPML STANIMVAQD GSGNYKTINE AVTVGLMRSD TTRFIIYIKA
GTYEENVEVG SKLENIAFVG DGIGKTIITG SKSNAGGFTT FNSATVAVDG DGFIAQDITF
RNTAGSANHQ AVALRSSSDL SVFYRCGFEG YQDTLFVHSK RQFYKECDIY GTTDFIFGNA
AVVFHNCNIY VRNPPNKVNT ITAQGRTDPN QNTGISILNC KVIADSELIL VQSSVKTYLG
RPWQKYSRTV FMMTYLDGLI DSAGWLEWDG DFALDTLYYG EYMNTGPRSS TTNRVTWAGY
HVITSTTEAS KFTIGNLIPG GTWLLATGMP NPS
//
