ID V9Q4E2_9CUCU Unreviewed; 370 AA.
AC V9Q4E2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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};
DE Flags: Fragment;
OS Sphenophorus levis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Dryophthorinae; Sphenophorus.
OX NCBI_TaxID=572107 {ECO:0000313|EMBL:AHC08663.1};
RN [1] {ECO:0000313|EMBL:AHC08663.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fat body {ECO:0000313|EMBL:AHC08663.1};
RA Evangelista D.E., Fonseca Pereira de Paula F., Henrique-Silva F.;
RT "Pectinases from the sugarcane weevil Sphenophorus levis: Putative
RT digestive accessory enzymes.";
RL Submitted (SEP-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; KF697075; AHC08663.1; -; Genomic_DNA.
DR AlphaFoldDB; V9Q4E2; -.
DR UniPathway; UPA00545; UER00823.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
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:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-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};
KW Hydrolase {ECO:0000256|RuleBase:RU000589, ECO:0000313|EMBL:AHC08663.1}.
FT DOMAIN 144..297
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHC08663.1"
FT NON_TER 370
FT /evidence="ECO:0000313|EMBL:AHC08663.1"
SQ SEQUENCE 370 AA; 39636 MW; 49A07B9336409E64 CRC64;
NQNPPGTSSR PILTASEANY YTKEKYLQGW SPPSISTNHT DYTVGGGGYS TIQAAVNDAI
NAGGSNRKYI KINTGTYQQV VYIPNTNVPL TIYGAGSRPD NTVITLNMPA QTTPSAYKNL
VNPNDAFFKP GDPAYSIYNG CASSSGTIGT SCSTVFWVLA PNVQIVNLQI QNSAKNKGDQ
QAVALQTNSD RIQVHNVNLL GHQDTLCAGS GGTDTQIAHY TNTYIEGDID YVFGGGTAIF
ESCTFYSKAD RKNDESVIFA PDTDPHQMYG YLVIKSTITG DSAWSSSKKV YLGRSWDAGV
KSANAYVPGT SPNGQLVIRE TTINGIVPNS APWTTATSGR AYAGNAANSR DLNNQNFNRF
WEYANTGSGA
//
