ID   PLYX_PECCA              Reviewed;         238 AA.
AC   P16530;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Putative pectate lyase X;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=PEL X;
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Er 18;
RA   Ito K., Kobayashi R., Nikaido N., Izaki K.;
RT   "DNA structure of pectate lyase I gene cloned from Erwinia carotovora.";
RL   Agric. Biol. Chem. 52:479-487(1988).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
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   -!- INDUCTION: By pectin.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; D00218; BAA00156.1; -; Genomic_DNA.
DR   AlphaFoldDB; P16530; -.
DR   SMR; P16530; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   UniPathway; UPA00545; UER00824.
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   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Lyase; Metal-binding; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..238
FT                   /note="Putative pectate lyase X"
FT                   /id="PRO_0000024855"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  26094 MW;  46800EBA1CF41B64 CRC64;
     MKYLLPTAAA GLLLLAAQPA MAANTGGYAT TDGGEVSGAV KKTARSMKEI VDIIEAAQVD
     SKGKKVKGGA YPLIITYSGN EDSLIKAAEK NICGQWSKDA RGVQIKEFTK GTYYPGHQWL
     IRQLRCLDCE TLLTLWYVIC ALAICQAARK HGDAIRIDNS PNVWIDHNEI FAKNFECKGT
     PDNDTTFESA VDIKKGSTNV TVSVSVKEVG TLVNLSRLFF PFRIQRYRAF RLPVSCLP