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Database: UniProt
Entry: S8C6L3_9LAMI
LinkDB: S8C6L3_9LAMI
Original site: S8C6L3_9LAMI 
ID   S8C6L3_9LAMI            Unreviewed;       508 AA.
AC   S8C6L3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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;
GN   ORFNames=M569_12391 {ECO:0000313|EMBL:EPS62394.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS62394.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS62394.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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|ARBA:ARBA00004191}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS62394.1}.
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DR   EMBL; AUSU01006172; EPS62394.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8C6L3; -.
DR   OrthoDB; 668039at2759; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
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   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   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   PANTHER; PTHR31707:SF188; PECTINESTERASE_PECTINESTERASE INHIBITOR 7-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}; Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Hydrolase {ECO:0000256|RuleBase:RU000589};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512}.
FT   DOMAIN          1..150
FT                   /note="Pectinesterase inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00856"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS62394.1"
FT   NON_TER         508
FT                   /evidence="ECO:0000313|EMBL:EPS62394.1"
SQ   SEQUENCE   508 AA;  54623 MW;  8451BF9A94E1E8E1 CRC64;
     PSTPCNSTPY PTYCSAVVGN SSAGNVHYYG RVSVGKSISA AWRFLGLINS YLRRSKSLTV
     TAVRALQDCQ FLAESNIDYL LSSSQLVNQT SQVLPQGDAD EVQTLLSAII TNTETCIDGL
     QATASAWSFR NGIITPLSSD TRLYSVSLAL VTEGWVPKAK RLQPRAKKLN GRRLLQVGVP
     STAGGGSGVV VVSDSVVVTQ DGSGNFTTIS DAVNAAPDNS DGSGGYFVIH VGAGVYEEYV
     SVPKNKRYVM MIGEGINRTI ITGNRSVDDG WTTFSSPTFA VVGKGFVAAN ITFQNTAGAI
     KHQAVAVRNG ADLSAFYNCS FEGFQDTLYA HSLRQFYSHC DIYGTVDFIF GNAAAVFQDC
     NIYPRLPLMG QFNTITAQGR TDPNQNTGFS IQNCSVRAAD DLANSSFSVQ NYLGRPWKMY
     STAVVMESFL DRLINPAGWS AWSGDFGLNT SYYAEFANYG PGSNTTGRVN WPAFHLIDST
     AAQNFTVSEF LIGDQWLPGT GVPYTAGL
//
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