PLY3_PECAS
ID PLY3_PECAS Reviewed; 374 AA.
AC Q6CZT2; O31035; P14006; P29171; Q47470;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Pectate lyase 3;
DE EC=4.2.2.2;
DE AltName: Full=Pectate lyase C;
DE Short=PLC;
DE AltName: Full=Pectate lyase III;
DE Short=PEL III;
DE Flags: Precursor;
GN Name=pel3; Synonyms=pelC, pelCI; OrderedLocusNames=ECA4069;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C18;
RX PubMed=7773390; DOI=10.1099/13500872-141-4-873;
RA Bartling S., Wegener C., Olsen O.;
RT "Synergism between Erwinia pectate lyase isoenzymes that depolymerize both
RT pectate and pectin.";
RL Microbiology 141:873-881(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLADES
CC subfamily. {ECO:0000305}.
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DR EMBL; X81847; CAA57441.1; -; Genomic_DNA.
DR EMBL; BX950851; CAG76966.1; -; Genomic_DNA.
DR RefSeq; WP_011095543.1; NC_004547.2.
DR AlphaFoldDB; Q6CZT2; -.
DR SMR; Q6CZT2; -.
DR STRING; 218491.ECA4069; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR EnsemblBacteria; CAG76966; CAG76966; ECA4069.
DR GeneID; 57210733; -.
DR KEGG; eca:ECA4069; -.
DR PATRIC; fig|218491.5.peg.4139; -.
DR eggNOG; COG3866; Bacteria.
DR HOGENOM; CLU_021894_2_1_6; -.
DR OMA; DMIRVDD; -.
DR OrthoDB; 660314at2; -.
DR UniPathway; UPA00545; UER00824.
DR Proteomes; UP000007966; 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 3: Inferred from homology;
KW Calcium; Disulfide bond; Lyase; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..374
FT /note="Pectate lyase 3"
FT /id="PRO_0000234450"
FT ACT_SITE 239
FT /evidence="ECO:0000255"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 93..176
FT /evidence="ECO:0000250"
FT DISULFID 350..373
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="T -> A (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="A -> V (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="N -> D (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="N -> K (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="E -> A (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="K -> N (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Y -> L (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="I -> V (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..78
FT /note="YN -> FI (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="N -> A (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> I (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="I -> L (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..135
FT /note="VI -> IV (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Q -> A (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="V -> I (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="I -> V (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> P (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> S (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> N (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="P -> A (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="K -> Q (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> S (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="T -> S (in Ref. 1; CAA57441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40682 MW; 9F404E0B3689724F CRC64;
MKYLLPSTAA GLLLLAAQPT MAANTGGYAT TDGGNVAGAV NKTARSMQDI IDIIEEAKLD
SKGKKVKGGA YPLIITYNGN EDALIKAAEN NICGQWSKDA RGVEIKEFTK GVTIIGTNGS
SANFGIWLTK SSDVIIRNMR FGYMPGGAQD GDAIRIDNTP NVWIDHNEIF AKNFECQGTK
DGDTTFESAI DIKKASTNVT VSYNYIHGIK KVGLSGFSSS DTGRDLTYHH NIYDDVNARL
PLQRGGQVHA YNNLYTGITS SGLNVRQKGI ALIERNWFEN AKNPVTSRYD GSNFGTWELR
NNNIMSPADF AKYNITWDKD TKAYVNAEDW KSTGTFASVP YSYSPVSPQC VKDKLANYAG
VNKNLAVLTA ANCN
