ID   PLYB_COLGL              Reviewed;         331 AA.
AC   O59939;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Pectate lyase B;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=PLB;
OS   Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=474922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CG-14;
RA   Wattad C., Keen N.T.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a virulence factor active in plant tissue maceration.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF052632; AAD09857.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59939; -.
DR   SMR; O59939; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   UniPathway; UPA00545; UER00824.
DR   PHI-base; PHI:222; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Calcium; Glycoprotein; Lyase; Metal-binding; Secreted; Signal; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..331
FT                   /note="Pectate lyase B"
FT                   /id="PRO_0000024895"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000255"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  35108 MW;  475A76F2525D4689 CRC64;
     MKFTGSPLLW PSWLPLPAPP PPLPSVTRRR DPRTVGKRAA ITDACDVGYG AGTTGGSGGT
     TTTVSTPAQF TAAATSDEKA VIVVKGAITG ATKVKVGSNK SIIGRAGSSL TGVGLYINKQ
     ENVIVRNMKI SKVLADNGDR IGIQASSKVW VDHCDLSSDK KNNGKDYYDG LLDITHASMA
     VTVSNTYIHD HYKGSLVGHS DSNSAEDTGK LYVTYANNHW YNVASRNPSV RFGNVHIFNN
     YAEKLETSGV NTRMGAQLLI ESSVFSDTKK AVTFLDSKST GYAVVNDVDL GGSTNDRPQG
     TFTKPDYSYT LLGSSKVKAA VVGTAGQTLT F