ID   PLYA_PAEBA              Reviewed;         222 AA.
AC   Q9X6Z2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Pectate lyase A;
DE            EC=4.2.2.2;
DE   AltName: Full=Pectin lyase;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelA;
OS   Paenibacillus barcinonensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=198119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY,
RP   COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=10658655; DOI=10.1099/00221287-146-1-89;
RA   Soriano M., Blanco A., Diaz P., Pastor F.I.J.;
RT   "An unusual pectate lyase from a Bacillus sp. with high activity on pectin:
RT   cloning and characterization.";
RL   Microbiology 146:89-95(2000).
RN   [2]
RP   FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=16514142; DOI=10.1099/mic.0.28562-0;
RA   Soriano M., Diaz P., Pastor F.I.J.;
RT   "Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with
RT   activity on highly methylated pectin.";
RL   Microbiology 152:617-625(2006).
CC   -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and
CC       pectins of methyl esterification degree from 22 to 89%, with an endo
CC       mode of action. In contrast to the majority of pectate lyases, displays
CC       high activity on highly methylated pectins. Is not able to cleave
CC       trigalacturonate. Does not degrade xylans and carboxymethylcellulose
CC       (CMC). {ECO:0000269|PubMed:10658655, ECO:0000269|PubMed:16514142}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:10658655, ECO:0000269|PubMed:16514142};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10658655,
CC       ECO:0000269|PubMed:16514142};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Ba(2+). To a lesser extent,
CC       is also inhibited by Sn(2+), Mg(2+) and Ag(+). Inhibited by EDTA in
CC       vitro. {ECO:0000269|PubMed:10658655}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=102.4 umol/min/mg enzyme with 22% esterified pectin as substrate
CC         {ECO:0000269|PubMed:10658655, ECO:0000269|PubMed:16514142};
CC         Vmax=95.4 umol/min/mg enzyme with polygalacturonic acid as substrate
CC         {ECO:0000269|PubMed:10658655, ECO:0000269|PubMed:16514142};
CC       pH dependence:
CC         Optimum pH is 10. Is stable for 1 hour at 40 degrees Celsius in the
CC         pH range 4.0-8.0. {ECO:0000269|PubMed:10658655,
CC         ECO:0000269|PubMed:16514142};
CC       Temperature dependence:
CC         Optimum temperature is 50-55 degrees Celsius. More than 50% of
CC         maximum activity is found in the temperature range 40-60 degrees
CC         Celsius. Retains more than 50% of the initial activity after 4 hours
CC         incubation at 40 degrees Celsius at pH 10, while at 50 degrees
CC         Celsius only 1% of the initial activity is found after the same
CC         treatment. {ECO:0000269|PubMed:10658655,
CC         ECO:0000269|PubMed:16514142};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ237980; CAB40884.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X6Z2; -.
DR   SMR; Q9X6Z2; -.
DR   CAZy; PL3; Polysaccharide Lyase Family 3.
DR   UniPathway; UPA00545; UER00824.
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:0047490; F:pectin 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; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR33407; PTHR33407; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Calcium; Lyase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..222
FT                   /note="Pectate lyase A"
FT                   /id="PRO_5000065163"
SQ   SEQUENCE   222 AA;  23233 MW;  7F29F585791C9682 CRC64;
     MKKMLTLLLS AGLVASIFGV MPAAAAPTVV NSTIVVPKGT TYDGQGKTFV ANPSTLGDGS
     QAENQKPVFR LEAGATLKNV IIGAPAADGV HCYGSCNISN VVWEDVGEDA LTLKSSGTVN
     ITGGAAYKAY DKVFQMNASG TINIKNFRAD DIGKLVRQNG GTSYAVNMTL DNSNISNVKD
     SIMRTDSSVS QGKITNTRYS KVPTLFKGFA SGKTSQSGNT QY