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 02-SEP-2026, entry version 130. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P11073; -. DR MDposit; 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: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; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; PECTATE LYASE 18-RELATED; 1. DR PANTHER; PTHR31683:SF18; PECTATE LYASE 21-RELATED; 1. DR Pfam; PF00544; Pectate_lyase_4; 1. DR SMART; SM00656; Amb_all; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. 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 PCDDB; P11073; -. 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 309..314 FT /evidence="ECO:0007829|PDB:1AIR" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:1O88" FT HELIX 346..348 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 //