ID G2ZR81_9RALS Unreviewed; 376 AA.
AC G2ZR81;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=Pectate lyase {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009};
GN Name=popW {ECO:0000313|EMBL:CCA81546.1};
GN ORFNames=BDB_150104 {ECO:0000313|EMBL:CCA81546.1};
OS blood disease bacterium R229.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=741978 {ECO:0000313|EMBL:CCA81546.1};
RN [1] {ECO:0000313|EMBL:CCA81546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R229 {ECO:0000313|EMBL:CCA81546.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA81546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R229 {ECO:0000313|EMBL:CCA81546.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU367009}.
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|RuleBase:RU367009};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|RuleBase:RU367009};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367009}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC {ECO:0000256|ARBA:ARBA00006463, ECO:0000256|RuleBase:RU367009}.
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DR EMBL; FR854071; CCA81546.1; -; Genomic_DNA.
DR AlphaFoldDB; G2ZR81; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule.
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 Pfam; PF03211; Pectate_lyase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU367009};
KW Lyase {ECO:0000256|RuleBase:RU367009, ECO:0000313|EMBL:CCA81546.1};
KW Secreted {ECO:0000256|RuleBase:RU367009}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 39567 MW; D614A3ECAA39F939 CRC64;
MSIQIDRPNN QFHMPTTWNH DAGSQIDTSQ LQRAVQLLEQ VLQQVQASKL FGNVLNQPEF
GNSGQGHGGS HGGGHHGGPT GFGENGRFGS PNAKPPAQPD IELPANKPNN GKHNTSAPTT
ETTPPAASPT PGTSPTSTPT TEGKVTYGAT PPNYSGEVDV SKPIVVKAGE TFDGKNQYFR
PTKEMGDGSQ NEHQKPLFIL EPGATLKNVQ YSGGDGIPLL GSAKLDRVVN RQVGEDAITI
DGAKNRAHDA KIAGIDPASI PGGTPKVEII NSAFYGAKDK VGQINGDVDL QVRGMYVNGA
GKVFRTNGGD TQIKATVNVQ DSNFQNVSEA VFRTDSKFST ASFSGDVKSD APFDGLAPNK
SQVNGTNKVS YKAYSG
//
