ID   A0A915N917_MELJA        Unreviewed;        71 AA.
AC   A0A915N917;
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=pectate lyase {ECO:0000256|ARBA:ARBA00012272};
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:scaffold9624_cov186.g14140};
RN   [1] {ECO:0000313|WBParaSite:scaffold9624_cov186.g14140}
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}.
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DR   WBParaSite; scaffold9624_cov186.g14140; scaffold9624_cov186.g14140; scaffold9624_cov186.g14140.
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   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   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   71 AA;  7618 MW;  40A1E16909393FA0 CRC64;
     XPIKGHVDFE YALITAAPNM RKSCDIKGAV DGQNILQIED GGSISNLIID DPAKGIWCEG
     SCTLTNVLYV I
//