ID   PLY1_PECCA              Reviewed;         374 AA.
AC   P0C1C0; P11430; P16529; Q06113; Q47468;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Pectate lyase 1;
DE            EC=4.2.2.2;
DE   AltName: Full=Pectate lyase A;
DE            Short=PLA;
DE   AltName: Full=Pectate lyase I;
DE            Short=PEL I;
DE   Flags: Precursor;
GN   Name=pel1; Synonyms=pelA;
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 PROTEIN SEQUENCE OF 23-32.
RC   STRAIN=Er;
RA   Ito K., Kobayashi R., Nikaido N., Izaki K.;
RT   "DNA structure of pectate lyase I gene cloned from Erwinia carotovora.";
RL   Agric. Biol. Chem. 52:479-487(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=Er;
RX   PubMed=1369060; DOI=10.1271/bbb.56.1596;
RA   Yoshida A., Matsuo Y., Kamio Y., Izaki K.;
RT   "Molecular cloning and sequencing of the extracellular pectate lyase II
RT   gene from Erwinia carotovora Er.";
RL   Biosci. Biotechnol. Biochem. 56:1596-1600(1992).
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; D00217; BAA00155.1; -; Genomic_DNA.
DR   EMBL; S51490; AAC60423.1; -; Genomic_DNA.
DR   PIR; JC1314; JC1314.
DR   RefSeq; WP_039492152.1; NZ_CP034938.1.
DR   AlphaFoldDB; P0C1C0; -.
DR   SMR; P0C1C0; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   GeneID; 51391439; -.
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                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           23..374
FT                   /note="Pectate lyase 1"
FT                   /id="PRO_0000024849"
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        10
FT                   /note="A -> L (in Ref. 1; BAA00155)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14..22
FT                   /note="LLAAQPTMA -> AARGPTDNG (in Ref. 1; BAA00155)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="I -> V (in Ref. 1; BAA00155)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144..159
FT                   /note="MPGGAKDGDAIRIDNS -> IRAAQKMAMPSVLITR (in Ref. 1; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="K -> N (in Ref. 1; BAA00155)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365..374
FT                   /note="LAVLTAANCK -> WRY (in Ref. 1; BAA00155)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  40153 MW;  7E60A2128D14E0D6 CRC64;
     MKYLLPSAAA GLLLLAAQPT MAANTGGYAT TDGGDVSGAV KKTARSLQEI VDIIEAAKKD
     SSGKAVKGGA YPLVITYNGN EDALIKAAEA NICGQWSKDP RGVEIKEFTK GITILGTNGS
     SANFGIWMVN SSNVVVRNMR FGYMPGGAKD GDAIRIDNSP NVWIDHNEIF AKNFECAGTP
     DNDTTFESAV DIKKGATNVT VSYNYIHGVK KVGLSGSSNT DTGRDLTYHH NIYSDVNSRL
     PLQRGGKVHA YNNLYDGIKS SGFNVRQKGI ALIESNWFEN ALNPVTARND DSNFGTWELR
     NNNITSPSDF AKYKITWGKP STPHINADDW KSTGKFPAVP YSYSPVSAQC VKDKLASYAG
     VGKNLAVLTA ANCK