PLYW_DICD3
ID PLYW_DICD3 Reviewed; 543 AA.
AC Q05526; E0SDC5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Pectate disaccharide-lyase;
DE EC=4.2.2.9 {ECO:0000250|UniProtKB:P22751};
DE AltName: Full=Exopolygalacturonate lyase;
DE Short=ExoPL;
GN Name=pelW; Synonyms=kdgC; OrderedLocusNames=Dda3937_03361;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=1766386; DOI=10.1111/j.1365-2958.1991.tb02149.x;
RA Condemine G., Robert-Baudouy J.;
RT "Analysis of an Erwinia chrysanthemi gene cluster involved in pectin
RT degradation.";
RL Mol. Microbiol. 5:2191-2202(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=3937;
RX PubMed=10383957; DOI=10.1128/jb.181.13.3912-3919.1999;
RA Shevchik V.E., Condemine G., Robert-Baudouy J., Hugouvieux-Cotte-Pattat N.;
RT "The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl,
RT two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi
RT 3937.";
RL J. Bacteriol. 181:3912-3919(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
CC -!- FUNCTION: Catalyzes the formation of unsaturated digalacturonates from
CC polygalacturonate or short oligogalacturonates.
CC {ECO:0000250|UniProtKB:P22751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) = 4-(4-deoxy-alpha-D-
CC galact-4-enuronosyl)-D-galacturonate + [(1->4)-alpha-D-
CC galacturonosyl](n-2); Xref=Rhea:RHEA:57104, Rhea:RHEA-COMP:14570,
CC Rhea:RHEA-COMP:14734, ChEBI:CHEBI:60189, ChEBI:CHEBI:140523;
CC EC=4.2.2.9; Evidence={ECO:0000250|UniProtKB:P22751};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC -!- PATHWAY: Glycan metabolism; pectin degradation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By galacturonate and PGA, and inhibited by EDTA.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 2 family.
CC {ECO:0000305}.
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DR EMBL; X62073; CAA43990.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98617.1; -; Genomic_DNA.
DR PIR; S17712; S17712.
DR RefSeq; WP_013318067.1; NC_014500.1.
DR AlphaFoldDB; Q05526; -.
DR SMR; Q05526; -.
DR STRING; 198628.Dda3937_03361; -.
DR CAZy; PL2; Polysaccharide Lyase Family 2.
DR EnsemblBacteria; ADM98617; ADM98617; Dda3937_03361.
DR GeneID; 9733852; -.
DR KEGG; ddd:Dda3937_03361; -.
DR PATRIC; fig|198628.6.peg.2395; -.
DR eggNOG; ENOG502Z7J0; Bacteria.
DR HOGENOM; CLU_036080_0_0_6; -.
DR OMA; GMPVYQF; -.
DR OrthoDB; 155856at2; -.
DR BioCyc; DDAD198628:DDA3937_RS11340-MON; -.
DR BioCyc; MetaCyc:MON-15658; -.
DR BRENDA; 4.2.2.9; 10687.
DR UniPathway; UPA00545; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ASAP.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IDA:ASAP.
DR GO; GO:0047489; F:pectate disaccharide-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0045490; P:pectin catabolic process; IDA:ASAP.
DR InterPro; IPR010702; Pectate_lyase_2.
DR Pfam; PF06917; Pectate_lyase_2; 1.
DR PIRSF; PIRSF001432; Pect_lyase; 1.
PE 2: Evidence at transcript level;
KW Copper; Cytoplasm; Lyase; Manganese; Nickel; Reference proteome.
FT CHAIN 1..543
FT /note="Pectate disaccharide-lyase"
FT /id="PRO_0000212998"
FT CONFLICT 534..543
FT /note="EFIYPEKLIH -> GIYLPRKINPLILFLQIHHY (in Ref. 2;
FT CAA43990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 62913 MW; 902EB7778352FC24 CRC64;
MSIFTDLNTS RKWQIDQWLS AVNSHIEKIQ QYGHSVVNPT PLLADGFEIK TQSPVVWQFP
DGHDAPISNF ASQQNWLRLL ISMSVITETE KYRHLAFCQS EYFLNRFVDE NSGLFYWGGH
RFINLDTLAS EGPESKSMVH ELKHHLPYYE FLHQVNPEKT RHFIQGFWNA HVEDWSCLDL
GRHGDYARQR DPDVFLHSRH DVVTPANWPE LPLTKGLTFV NAGTDLIYAA FVYARHTGDA
HAAAWGKHLY RQYVLARNPE TGMPVYQFSS PLQRQPVPAD DNQTQSWFGD RAQRQFGPEF
GAIAREANVL FRDMRPLLID NPLAMLDILR HQPDAEILTW VIAGLKNYYQ YAYDVNSNSL
RPMWNNGQDM TDYCFKRDGY YGKAGTVLKP FPLEGDYLLP LVRAWLLSDD DDLHTLIVTM
LSRLEKQGIH QSASPFLLLA ITELAHAKQS AQWAEYAWQM AEILFKRYFH HGLFVRSEHH
RYVRLDDPFP AILLTLIAAC RNKWSEVPAV LTQGGYIHGD YRINGESRVI YDTEFIYPEK
LIH
