ID   E2JE18_9BILA            Unreviewed;       270 AA.
AC   E2JE18;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Probable pectate lyase F {ECO:0000256|ARBA:ARBA00039895};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
OS   Meloidogyne enterolobii.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=390850 {ECO:0000313|EMBL:ADN87334.1};
RN   [1] {ECO:0000313|EMBL:ADN87334.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhuo K., Chi Y., Liao J.;
RT   "Cloning of a Meloidogyne enterolobii pectate lyase gene.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   EMBL; HQ180169; ADN87334.1; -; mRNA.
DR   AlphaFoldDB; E2JE18; -.
DR   SMR; E2JE18; -.
DR   CAZy; PL3; Polysaccharide Lyase Family 3.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
KW   Lyase {ECO:0000313|EMBL:ADN87334.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..270
FT                   /note="Probable pectate lyase F"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003159668"
FT   REGION          223..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  29874 MW;  B4EE4393B559F3D3 CRC64;
     MFTSKTSFNF LLISSLACLC KADWPTRRND IQVTETKQIT KFDCQFDRYI PDPSKLGNGN
     QDEHQKYVFD IKNGGSLSNC IIGARPGTKG SAHGIVCDGS CDVNNVWFED VGEDAINFNG
     DSDDCVYNVN GGGARDAEDK VMQFDGKGTL NIKNYYVNNY VRFCRSCGNC DDQHKRDIII
     TNLTAIKGQA GQFVCGVNSN YKDTCTLHDI KMEKGIHPCK VFTGNNDGSE PNSNNDEEDH
     GDGKYCIYKS GDIKYTGSKP KPKSKKSAKN
//