ID   A8E4A3_PSEVI            Unreviewed;       538 AA.
AC   A8E4A3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=pectate lyase {ECO:0000256|ARBA:ARBA00012272};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN   Name=hrpW {ECO:0000313|EMBL:AAX58535.1};
GN   ORFNames=PAI-R2-ORF24 {ECO:0000313|EMBL:AAX58535.1};
OS   Pseudomonas viridiflava.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=33069 {ECO:0000313|EMBL:AAX58535.1};
RN   [1] {ECO:0000313|EMBL:AAX58535.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PT210.1a {ECO:0000313|EMBL:AAX58535.1};
RX   PubMed=17720907; DOI=10.1534/genetics.107.077925;
RA   Araki H., Innan H., Kreitman M., Bergelson J.;
RT   "Molecular evolution of pathogenicity-island genes in Pseudomonas
RT   viridiflava.";
RL   Genetics 177:1031-1041(2007).
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:0000256|ARBA:ARBA00000695};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000256|ARBA:ARBA00006463}.
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DR   EMBL; AY859319; AAX58535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8E4A3; -.
DR   CAZy; PL3; Polysaccharide Lyase Family 3.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; PECTATE LYASE F-RELATED; 1.
DR   PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
FT   REGION          60..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  50912 MW;  3636A8011982687D CRC64;
     MSDLTSLSGS MGNLSSLPGV GGTSMGIGAS LAGAGQGAQG GQSALQELAG MLAEMLLGSG
     SGSGSGAGGG QSAGKTGQGG QSDLDSLLQS LQGNGQGGDK QTKDSGAAGG GEKELLTQVL
     MALFEKILGG SDSSSGAGNG SGGGSGGASG IGGGGTGASK DAGALGQGQG LGGTQGAAGG
     SSTEDLVNTL MQKLGGGSLD NSIQPTADGG GEVSQNGKLK ELLEMIAQFM DSHPETFNQP
     SDAAGKGGGG GTPSLGGGGG GGGGGGGGTP SVGGGGGGGG TPSLGGGGGG GGGTPSIGGG
     GGTPAPTGPT GTPSPTGPTG TGTSGSATPV SFPTASGTPT VVNETIKVGP GETFDGGGKT
     FTAGKALGDG GQGEGQKPMF ELAEGATLKN VVLGDNAADG VHVRAASEKA VNVDNVHWTN
     VGEDALTVKG EGGAKVTNLN ITNSSAQGAN DKVFQLNADA NVNVDNFKVK DFGTFMRTNG
     GQQGDWNLDL KNISAEDGKF SFVKSDSEGL NLTTSGIDLK NVENAYSKLP GSTNHKEA
//