ID PLY1_PECAS Reviewed; 374 AA. AC Q6CZT4; P11430; P16529; Q06113; Q47468; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 14-DEC-2022, entry version 98. 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; OrderedLocusNames=ECA4067; OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia OS carotovora subsp. atroseptica). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=218491; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-36. RC STRAIN=EC; RX PubMed=3371662; DOI=10.1016/0378-1119(88)90590-2; RA Lei S.-P., Lin H.-C., Wang S.-S., Wilcox G.; RT "Characterization of the Erwinia carotovora pelA gene and its product RT pectate lyase A."; RL Gene 62:159-164(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C18; RX PubMed=7773390; DOI=10.1099/13500872-141-4-873; RA Bartling S., Wegener C., Olsen O.; RT "Synergism between Erwinia pectate lyase isoenzymes that depolymerize both RT pectate and pectin."; RL Microbiology 141:873-881(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672; RX PubMed=15263089; DOI=10.1073/pnas.0402424101; RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.; RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora RT subsp. atroseptica and characterization of virulence factors."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA24845.1; Type=Erroneous initiation; Evidence={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; M18859; AAA24845.1; ALT_INIT; Genomic_DNA. DR EMBL; X81847; CAA57439.1; -; Genomic_DNA. DR EMBL; BX950851; CAG76964.1; -; Genomic_DNA. DR PIR; JT0242; WZWCP1. DR RefSeq; WP_011095541.1; NC_004547.2. DR AlphaFoldDB; Q6CZT4; -. DR SMR; Q6CZT4; -. DR STRING; 218491.ECA4067; -. DR CAZy; PL1; Polysaccharide Lyase Family 1. DR EnsemblBacteria; CAG76964; CAG76964; ECA4067. DR GeneID; 57210731; -. DR KEGG; eca:ECA4067; -. DR PATRIC; fig|218491.5.peg.4135; -. DR eggNOG; COG3866; Bacteria. DR HOGENOM; CLU_021894_2_1_6; -. DR OMA; DSADCIC; -. DR OrthoDB; 660314at2; -. DR UniPathway; UPA00545; UER00824. DR Proteomes; UP000007966; Chromosome. 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; PECTATE LYASE 18-RELATED; 1. DR Pfam; PF00544; Pectate_lyase_4; 1. DR SMART; SM00656; Amb_all; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. PE 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Disulfide bond; Lyase; Metal-binding; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:3371662" FT CHAIN 23..374 FT /note="Pectate lyase 1" FT /id="PRO_0000234448" 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 13 FT /note="L -> V (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 51..66 FT /note="VDIIEAAKKDSSGKVV -> INLIEEAQLDSKGKKL (in Ref. 1; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 65 FT /note="V -> A (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 71 FT /note="F -> Y (in Ref. 1; AAA24845 and 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="I -> L (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 128 FT /note="V -> L (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 128 FT /note="V -> M (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="V -> I (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="I -> V (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="A -> G (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 205 FT /note="F -> Y (in Ref. 1; AAA24845 and 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="Y -> H (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="Y -> H (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="N -> T (in Ref. 1; AAA24845)" FT /evidence="ECO:0000305" FT CONFLICT 256 FT /note="D -> G (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 314 FT /note="K -> N (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="S -> P (in Ref. 1; AAA24845 and 2; CAA57439)" FT /evidence="ECO:0000305" FT CONFLICT 357 FT /note="N -> S (in Ref. 2; CAA57439)" FT /evidence="ECO:0000305" SQ SEQUENCE 374 AA; 40178 MW; DDDA152B0F49CDDA CRC64; MKYLLPSAAA GLLLLAAQPT MAANTGGYAT TDGGDVSGAV KKTARSLQEI VDIIEAAKKD SSGKVVKGGA FPLVITYNGN EDALIKAAEA NICGQWSKDP RGVEIKEFTK GITILGTNGS SANFGIWVVN SSNVVVRNMR FGYMPGGAKD GDAIRIDNSP NVWIDHNEIF AKNFECAGTP DNDTTFESAV DIKKASTNVT VSYNFIHGVK KVGLSGSSNT DTGRNLTYHH NIYSDVNSRL PLQRGGQVHA YNNLYDGIKS SGFNVRQKGI ALIESNWFEN ALNPVTARND DSNFGTWELR NNNITSPSDF AKYKITWGKP STPHINADDW KSTGKFPAVS YSYSPVSAQC VKDKLANYAG VGKNQAVLTA ANCK //