ID   PLYD_DICCH              Reviewed;         391 AA.
AC   P18209;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Pectate lyase D;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelD;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B374;
RX   PubMed=2615652; DOI=10.1111/j.1365-2958.1989.tb00124.x;
RA   van Gijsegem F.;
RT   "Relationship between the pel genes of the pelADE cluster in Erwinia
RT   chrysanthemi strain B374.";
RL   Mol. Microbiol. 3:1415-1424(1989).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLBC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X17284; CAA35176.1; -; Genomic_DNA.
DR   PIR; S06969; S06969.
DR   AlphaFoldDB; P18209; -.
DR   SMR; P18209; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PRIDE; P18209; -.
DR   BRENDA; 4.2.2.2; 2141.
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: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; Lyase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..31
FT   CHAIN           32..391
FT                   /note="Pectate lyase D"
FT                   /id="PRO_0000024856"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255"
FT   BINDING         170
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  42066 MW;  C8EEF1C9493F2ABC CRC64;
     MNNTRVSFRS TKSLLAAIIA TSMMTWSVNR ATLQTTKATE AASTGWATQG GTTGGAKAAS
     AKIYAVKNIS EFKAALNGTD TDPKIIQVTG AIDISGGKAY TSFDDQKARS QISVPSNTTI
     IGIGSNGKFT NGSLVIKGVS NVILRNLYIE TPVDVAPHYE EGDGWNAEWD AAVIDNSTRV
     WVDHVTISDG SFTDDKYTTK NGEKYVQHDG ALDIKKGSDY VTISSSRFEL HDKTILIGHS
     DSNGSQDSGK LRVTFHNNVF DRVTERTPRV RFGSIHAYNN VYLGDVKNSV YPYLYSFGLG
     TSGTILSESN SFTLSNLKSI DGKNPECSIV KQFNSKVFSD NGSLVNGSST TKLDTCAVTA
     YKPTLPYKYS AQTMTSSLAS SINSNAGYGK L