ID   PLY3_PECCA              Reviewed;         374 AA.
AC   P0C1C2; O31035; P14006; P29171; Q47470;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
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;
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Er;
RX   PubMed=1368679; DOI=10.1271/bbb1961.55.933;
RA   Yoshida A., Izuta M., Ito K., Kamio Y., Izaki K.;
RT   "Cloning and characterization of the pectate lyase III gene of Erwinia
RT   carotovora Er.";
RL   Agric. Biol. Chem. 55:933-940(1991).
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; D10064; BAA00953.1; -; Genomic_DNA.
DR   PIR; JU0462; WZWCP3.
DR   AlphaFoldDB; P0C1C2; -.
DR   SMR; P0C1C2; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
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; 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; Direct protein sequencing; Disulfide bond; Lyase; Metal-binding;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..374
FT                   /note="Pectate lyase 3"
FT                   /id="PRO_0000024851"
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"
SQ   SEQUENCE   374 AA;  40480 MW;  1D12415917AA1B23 CRC64;
     MKYLLPSAAA GLLLLAAQPT MAANTGGYAT TDGGDVAGAV KKTARSMQDI IDIIEAAKLD
     SNGKKVKGGA YPLVITYNGN EDALIKAAEA NICGQWSKDA RGVEIKEFTK GITIIGTNGS
     SANFGIWLTK SSDIVIRNMR FGYMPGGAQD GDAIRIDNTP NVWIDHNEIF AKNFECAGTK
     DGDTTFESAI DIKKASTNVT ISYNYIHGIK KVGLSGFSSS DTGRDLTYHH NIYDDVNARL
     PLQRGGQVHA YNNLYTGITS SGLNVRQKGI ALIERNWFEN AKNPVTSRYD GSNFGTWELR
     NNNVMSPADF AKYNITWDKD SKPYVNAEDW KSTGTFASVP YSYSPVSAQC VKDKLANYAG
     VNKNLAVLTA ANCN