PLYC_DICCH
ID PLYC_DICCH Reviewed; 375 AA.
AC P11073;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Pectate lyase C;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN Name=pelC {ECO:0000303|PubMed:3042750};
OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=556;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC16;
RX PubMed=3042750; DOI=10.1128/jb.170.8.3468-3478.1988;
RA Tamaki S.J., Gold S., Robeson M., Manulis S., Keen N.T.;
RT "Structure and organization of the pel genes from Erwinia chrysanthemi
RT EC16.";
RL J. Bacteriol. 170:3468-3478(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-375.
RX PubMed=8502994; DOI=10.1126/science.8502994;
RA Yoder M.D., Keen N.T., Jurnak F.;
RT "New domain motif: the structure of pectate lyase C, a secreted plant
RT virulence factor.";
RL Science 260:1503-1507(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-375.
RX PubMed=12226275; DOI=10.1104/pp.111.1.73;
RA Lietzke S.E., Scavetta R.D., Yoder M.D., Jurnak F.A.;
RT "The refined three-dimensional structure of pectate lyase E from Erwinia
RT chrysanthemi at 2.2-A resolution.";
RL Plant Physiol. 111:73-92(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-375 IN COMPLEX WITH CALCIUM,
RP AND COFACTOR.
RX PubMed=12540845; DOI=10.1074/jbc.m209306200;
RA Herron S.R., Scavetta R.D., Garrett M., Legner M., Jurnak F.;
RT "Characterization and implications of Ca2+ binding to pectate lyase C.";
RL J. Biol. Chem. 278:12271-12277(2003).
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;
CC Evidence={ECO:0000269|PubMed:12540845};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12540845};
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; M19411; AAA24849.1; -; Genomic_DNA.
DR PIR; A31091; WZWC6C.
DR RefSeq; WP_039999250.1; NZ_JAFCAF010000023.1.
DR PDB; 1AIR; X-ray; 2.20 A; A=23-375.
DR PDB; 1O88; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8D; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8E; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8F; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8G; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8H; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8I; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8J; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8K; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8L; X-ray; 2.20 A; A=23-375.
DR PDB; 1O8M; X-ray; 2.20 A; A=23-375.
DR PDB; 1PLU; X-ray; 2.20 A; A=23-375.
DR PDB; 2EWE; X-ray; 2.20 A; A=23-375.
DR PDB; 2PEC; X-ray; 2.20 A; A=23-375.
DR PDBsum; 1AIR; -.
DR PDBsum; 1O88; -.
DR PDBsum; 1O8D; -.
DR PDBsum; 1O8E; -.
DR PDBsum; 1O8F; -.
DR PDBsum; 1O8G; -.
DR PDBsum; 1O8H; -.
DR PDBsum; 1O8I; -.
DR PDBsum; 1O8J; -.
DR PDBsum; 1O8K; -.
DR PDBsum; 1O8L; -.
DR PDBsum; 1O8M; -.
DR PDBsum; 1PLU; -.
DR PDBsum; 2EWE; -.
DR PDBsum; 2PEC; -.
DR AlphaFoldDB; P11073; -.
DR PCDDB; P11073; -.
DR SMR; P11073; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR BRENDA; 4.2.2.2; 2141.
DR UniPathway; UPA00545; UER00824.
DR EvolutionaryTrace; P11073; -.
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 3D-structure; Calcium; Disulfide bond; Lyase; Metal-binding; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..22
FT CHAIN 23..375
FT /note="Pectate lyase C"
FT /id="PRO_0000024854"
FT ACT_SITE 240
FT /evidence="ECO:0000255"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12540845"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12540845"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12540845"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12540845"
FT DISULFID 94..177
FT DISULFID 351..374
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1AIR"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1O8E"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 278..288
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1AIR"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:1AIR"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1AIR"
SQ SEQUENCE 375 AA; 39944 MW; F76DD8195A35B886 CRC64;
MKSLITPITA GLLLALSQPL LAATDTGGYA ATAGGNVTGA VSKTATSMQD IVNIIDAARL
DANGKKVKGG AYPLVITYTG NEDSLINAAA ANICGQWSKD PRGVEIKEFT KGITIIGANG
SSANFGIWIK KSSDVVVQNM RIGYLPGGAK DGDMIRVDDS PNVWVDHNEL FAANHECDGT
PDNDTTFESA VDIKGASNTV TVSYNYIHGV KKVGLDGSSS SDTGRNITYH HNYYNDVNAR
LPLQRGGLVH AYNNLYTNIT GSGLNVRQNG QALIENNWFE KAINPVTSRY DGKNFGTWVL
KGNNITKPAD FSTYSITWTA DTKPYVNADS WTSTGTFPTV AYNYSPVSAQ CVKDKLPGYA
GVGKNLATLT STACK
