ID   PLYA_PAEAM              Reviewed;         222 AA.
AC   D3JTC1;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Pectate lyase A {ECO:0000303|PubMed:20622125};
DE            EC=4.2.2.2 {ECO:0000269|PubMed:20622125};
DE   AltName: Full=Pectin lyase {ECO:0000305|PubMed:20622125};
DE            EC=4.2.2.10 {ECO:0000269|PubMed:20622125};
DE   Flags: Precursor;
GN   Name=pelA {ECO:0000303|PubMed:20622125};
OS   Paenibacillus amylolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=27C64;
RX   PubMed=20622125; DOI=10.1128/aem.00043-10;
RA   Boland W.E., Henriksen E.D., Doran-Peterson J.;
RT   "Characterization of two Paenibacillus amylolyticus strain 27C64 pectate
RT   lyases with activity on highly methylated pectin.";
RL   Appl. Environ. Microbiol. 76:6006-6009(2010).
CC   -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and
CC       pectins with low (20-34%) and high (90%) levels of methyl
CC       esterification, with an endo mode of action. In contrast to the
CC       majority of pectate lyases, displays high activity on highly methylated
CC       pectins. Does not show xylanase and cellulase activity.
CC       {ECO:0000269|PubMed:20622125}.
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:0000269|PubMed:20622125};
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         Evidence={ECO:0000269|PubMed:20622125};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:20622125};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 10.5. {ECO:0000269|PubMed:20622125};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:20622125};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation.
CC       {ECO:0000269|PubMed:20622125}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; GU289919; ADB78774.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3JTC1; -.
DR   SMR; D3JTC1; -.
DR   CAZy; PL3; Polysaccharide Lyase Family 3.
DR   BRENDA; 4.2.2.2; 632.
DR   UniPathway; UPA00545; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0030570; F:pectate lyase activity; IDA:UniProtKB.
DR   GO; GO:0047490; F:pectin lyase activity; IDA:UniProtKB.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
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; Carbohydrate metabolism; Lyase; Polysaccharide degradation;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..222
FT                   /note="Pectate lyase A"
FT                   /id="PRO_5003047386"
SQ   SEQUENCE   222 AA;  23253 MW;  654FFA2C2EFE1918 CRC64;
     MKKMLTLLLS AGLVASIFGV MPAAAAPTVV NSTIVVPKGT TYDGQGKTFV ANPSTLGDGS
     QAENQKPVFR LEAGATLKNV IIGAPAADGV HCYGNCNISN VVWQDVGEDA LTLKSSGTVN
     ITGGAAYKAY DKVFQINAAG TINIKNFRAD DIGKLVRQNG GTTFTVNMTL DNSNISNVKD
     AIMRTDSSSS QGRITNTRYS KVPTLFKGFA SGKTSQSGNT QY