PLYA_DICD3
ID PLYA_DICD3 Reviewed; 392 AA.
AC P0C1A3; E0SAZ1; P29155;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Pectate lyase A {ECO:0000303|PubMed:1593262};
DE EC=4.2.2.2 {ECO:0000269|PubMed:1593262};
DE Flags: Precursor;
GN Name=pelA {ECO:0000303|PubMed:1593262}; OrderedLocusNames=Dda3937_03370;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=3937;
RX PubMed=1593262; DOI=10.1099/00221287-138-3-499;
RA Favey S., Bourson C., Bertheau Y., Kotoujansky A., Boccara M.;
RT "Purification of the acidic pectate lyase and nucleotide sequence of the
RT corresponding gene (pelA) of Erwinia chrysanthemi strain 3937.";
RL J. Gen. Microbiol. 138:499-508(1992).
RN [2]
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: Involved in maceration and soft-rotting of plant tissue.
CC {ECO:0000250}.
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:0000269|PubMed:1593262};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:1593262};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P11073};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1593262}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLADES
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77808; AAA24846.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM99550.1; -; Genomic_DNA.
DR PIR; A44852; A44852.
DR RefSeq; WP_013318981.1; NC_014500.1.
DR AlphaFoldDB; P0C1A3; -.
DR SMR; P0C1A3; -.
DR STRING; 198628.Dda3937_03370; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR EnsemblBacteria; ADM99550; ADM99550; Dda3937_03370.
DR GeneID; 9734801; -.
DR KEGG; ddd:Dda3937_03370; -.
DR PATRIC; fig|198628.6.peg.3307; -.
DR eggNOG; COG3866; Bacteria.
DR HOGENOM; CLU_021894_3_0_6; -.
DR OMA; DDMYTTK; -.
DR OrthoDB; 163648at2; -.
DR BioCyc; DDAD198628:DDA3937_RS15610-MON; -.
DR BioCyc; MetaCyc:MON-15663; -.
DR UniPathway; UPA00545; UER00824.
DR PHI-base; PHI:6853; -.
DR Proteomes; UP000006859; Chromosome.
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; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PTHR31683; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Lyase; Metal-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..392
FT /note="Pectate lyase A"
FT /id="PRO_0000233030"
FT ACT_SITE 272
FT /evidence="ECO:0000255"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11073"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11073"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11073"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11073"
FT DISULFID 329..357
FT /evidence="ECO:0000250"
SQ SEQUENCE 392 AA; 41555 MW; 7EC15FB476B9D333 CRC64;
MNKVSGRSFT RTSTCLLATL IAGVMTSGVS AAELVNSKAL ESAPAAGWAS QNGSTTGGAA
ATSDNIYVVT NISEFTSALS AGAVAKIIQI TGTVDISGGT PYKDFADQKA RSQINIPANT
TVIGIGTDAK FINGSLIIDG TDGTNNVIIR NVYIQTPIDV EPHYEKGDGW NAEWDGMNIT
NGAHHVWVDH VTISDGSFTD DMYTTKDGET YVQHDGALDI KRGSDYVTIS NSLFDQHDKT
MLIGHSDTNS AQDKGKLHVT LFNNVFNRVT ERAPRVRYGS IHSFNNVFNG DVKDPVYRYL
YSFGIGTSGS VLSEGNSFTI ANLSASKACK VVKKFNGSIF SDNGSVLNGS AADLSGCGFS
AYTSAIPYVY AVQPMTTELA QSITDHAGSG KL
