ID   A0A915LVV0_MELJA        Unreviewed;       226 AA.
AC   A0A915LVV0;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 9.
DE   RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
OS   Meloidogyne javanica (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne; Meloidogyne incognita group.
OX   NCBI_TaxID=6303 {ECO:0000313|Proteomes:UP000887561, ECO:0000313|WBParaSite:scaffold1794_cov184.g3650};
RN   [1] {ECO:0000313|WBParaSite:scaffold1794_cov184.g3650}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
CC   -!- FUNCTION: Pectinolytic enzyme consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins. Favors pectate, the
CC       anion, over pectin, the methyl ester. {ECO:0000256|ARBA:ARBA00025679}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000695};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000256|ARBA:ARBA00006463}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   WBParaSite; scaffold1794_cov184.g3650; scaffold1794_cov184.g3650; scaffold1794_cov184.g3650.
DR   Proteomes; UP000887561; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:TreeGrafter.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR   PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887561};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ   SEQUENCE   226 AA;  24692 MW;  0591F87DB8112C5F CRC64;
     MISILLIIFG KYLDCGYNRY VPNLKNGKWG SGEFMFPVFQ LQDGATIKRC IFSGADGIHC
     NGTCLVEDCW NENVADDSIT LLGNNPSAVY TIQGGGAKNG KGKIIQFDGA GTLNVNNFYI
     HTCGEGIRSC GNCLSQYRNR KINVNGLTIE NLQAGQYVVG VNKNYGDQAT LKNIHILGPT
     ANQVFPCKVF EGNNQGKNPN VLVMENNKGG DGTYCIYDES DIHIWS
//