PLYL_DICCH
ID PLYL_DICCH Reviewed; 425 AA.
AC P0C1A6; Q47473; Q59421;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Pectate lyase L {ECO:0000250|UniProtKB:P0C1A7};
DE EC=4.2.2.2 {ECO:0000250|UniProtKB:P0C1A7};
DE AltName: Full=Pectate transeliminase {ECO:0000250|UniProtKB:P0C1A7};
DE Flags: Precursor;
GN Name=pelL;
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=EC16;
RX PubMed=7635842; DOI=10.1128/jb.177.15.4553-4556.1995;
RA Alfano J.R., Ham J.H., Collmer A.;
RT "Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine-
RT rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with
RT deletions affecting the major pectate lyase isozymes.";
RL J. Bacteriol. 177:4553-4556(1995).
CC -!- FUNCTION: Presents an endo-cleaving activity on polygalacturonate or
CC partially methylated pectin. {ECO:0000250|UniProtKB:P0C1A7}.
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:0000250|UniProtKB:P0C1A7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P0C1A7};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5. {ECO:0000250|UniProtKB:P0C1A7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C1A7}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC {ECO:0000305}.
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DR EMBL; L42248; AAA99476.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C1A6; -.
DR SMR; P0C1A6; -.
DR CAZy; PL9; Polysaccharide Lyase Family 9.
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; IPR039448; Beta_helix.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF13229; Beta_helix; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Lyase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..425
FT /note="Pectate lyase L"
FT /id="PRO_0000024936"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
FT DISULFID 28..114
FT /evidence="ECO:0000250|UniProtKB:P0C1A7"
SQ SEQUENCE 425 AA; 45537 MW; BE2557332CFF91F7 CRC64;
MKYLNCFIST GLAAFFLVNS TSVLAADCSS DLTSGISTKR IYYVAPNGSS SNNGNSFNSP
MSFTAAMAAA NPGELILLKP GTYTIPYTQG KGNTITFNKS GKEGSPIYVA AANCGRAVFD
FSFPDSQWVQ ASYGFYVTGD YWYFKGIEVT RAGYQGAYVT GSHNTFENTA FHHNRNTGLE
INNGGSYNTV INSDAYRNYD PKKNGSMADG FGPKQKQGQG NRFGGCRAWE NSDDGFDLFD
SPQKVVIENS WAFRNGINYW SDSSFAGNGN GFKLGGNQAV GNHRITRSVA FGNVSKGFDQ
NNNAGGVTVI NNTSYKNGIN YGFGSNVKSG QKHYFRNNVS LSGSATVNNA DAKSNSWDTG
PVASASDFVS LDTSLATISR DNDGTLPETA LFRLSTNSKL INAGTKESNI SYSGSAPDLG
AFERN
