ID   PLY3_PECCC              Reviewed;         374 AA.
AC   P0C1C3; 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 62.
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 subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=2695748; DOI=10.1111/j.1365-2958.1989.tb00164.x;
RA   Hinton J.C.D., Sidebotham J.M., Gill D.R., Salmond G.P.C.;
RT   "Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia
RT   carotovora subspecies carotovora belong to different gene families.";
RL   Mol. Microbiol. 3:1785-1795(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LY34;
RA   Lim S.T., Park Y.W., Yun H.D.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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; X16398; CAA34433.1; -; Genomic_DNA.
DR   EMBL; AF026033; AAB82289.1; -; Genomic_DNA.
DR   PIR; S07652; WZWCPC.
DR   RefSeq; WP_010297068.1; NZ_JUJS01000003.1.
DR   AlphaFoldDB; P0C1C3; -.
DR   SMR; P0C1C3; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   GeneID; 61346284; -.
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   3: Inferred from homology;
KW   Calcium; Disulfide bond; Lyase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..374
FT                   /note="Pectate lyase 3"
FT                   /id="PRO_0000234451"
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        90..91
FT                   /note="ND -> AN (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="K -> S (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="T -> V (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="S -> P (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="M -> Y (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="N -> D (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="T -> S (in Ref. 2; AAB82289)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  40565 MW;  34CE8929170CC21C CRC64;
     MKYLLPSAAA GLLLLAAQPT MAANTGGYAT TDGGDVAGAV KKTARSMQDI IDIIEAAKLD
     SNGKKVKGGA YPLVITYNGN EDALIKAAEN DICGQWKKDA RGVEIKEFTK GITIIGTNGS
     SANFGIWLTK SSDIVIRNMR FGYMPGGAQD GDAIRIDNTP NVWIDHNEIF AKNFECAGTK
     DGDTTFESAI DIKKASTNVT VSYNYIHGIK KVGLSGFSSS DTGRDLTYHH NIYDDVNARL
     PLQRGGQVHA YNNLYTGITS SGLNVRQKGI ALIERNWFEN AKNPVTSRYD GSNFGTWELR
     NNNVMSPADF AKYNITWDKD TKPYVNAEDW KSTGTFASVP YSYSPVSAQC VKDKLANYAG
     VNKNLAVLTA ANCN