ID   A8E429_PSEVI            Unreviewed;       544 AA.
AC   A8E429;
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:AAX58461.1};
GN   ORFNames=PAI-R2-ORF24 {ECO:0000313|EMBL:AAX58461.1};
OS   Pseudomonas viridiflava.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=33069 {ECO:0000313|EMBL:AAX58461.1};
RN   [1] {ECO:0000313|EMBL:AAX58461.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DUD4.5a {ECO:0000313|EMBL:AAX58461.1};
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; AY859282; AAX58461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8E429; -.
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..347
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        320..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  51397 MW;  E00B2B8CC58B4B53 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 GGTPSVGGGG GGGGTPSVGG GGGGGGTPSV GGGGGGGGGT
     PSIGGGGGTP APTGPTGTPS PTGPTGTGTS GSATPVSFPT ASGTPTVVNE TIKVGPGETF
     DGGGKTFTAG KALGDGGQGE GQKPMFELAE GATLKNVVLG DNAADGVHVR AASEKAVNVD
     NVHWTNVGED ALTVKGEGGA KVTNLNITNS SAQGANDKVF QLNADANVNV DNFKVKDFGT
     FMRTNGGQQG DWNLDLKNIS AEDGKFSFVK SDSEGLNLTT SGIDLKNVEN AYSKLPGSTN
     HKEA
//