ID A0A058ZWZ8_EUCGR Unreviewed; 344 AA.
AC A0A058ZWZ8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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_L00260 {ECO:0000313|EMBL:KCW45891.1};
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:KCW45891.1};
RN [1] {ECO:0000313|EMBL:KCW45891.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW45891.1};
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|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 -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; KK198769; KCW45891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZWZ8; -.
DR STRING; 71139.A0A058ZWZ8; -.
DR EnsemblPlants; KCW45891; KCW45891; EUGRSUZ_L00260.
DR Gramene; KCW45891; KCW45891; EUGRSUZ_L00260.
DR eggNOG; ENOG502QVK0; Eukaryota.
DR InParanoid; A0A058ZWZ8; -.
DR OMA; TEEHIIF; -.
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: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 PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF120; PECTINESTERASE 52-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 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}.
FT DOMAIN 39..328
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 344 AA; 38649 MW; 03A98E8A2A0E226E CRC64;
MKSAWHSETM NFFFGKKKML YCDFKLNCNI MDTNYGNTIT VDQHGSGHFT SVQVAINSVP
SGNNKWISIR INPGTYKEMV TIPPDKPCIF LQGKGRDSTI ITYNSHEQTD TSATFTSSPD
NIVVQGITFK NSYNRYWKES NEPPLVQALA ARVYGDKCVF FECGFLGLQD TLWDVQGRHY
YGSCYIEGAI DFIFGSGQSI FEDCTMNVTA TLPPYRLQYS CITAQGRASP GDPSGFVFER
GAVIGSGPYL LGRAYGPYSR VVFHKTLLSA GVAPQGWDPW HCQGREDNIM YAEVDCEGTG
SDTSQRVQWE KHLDKTQLQY FSRSYFLDQE GWLANTPLGK TFES
//
