ID PEL1_ERWCT 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 05-MAY-2009, entry version 32. DE RecName: Full=Pectate lyase 1; DE EC=4.2.2.2; DE AltName: Full=Pectate lyase I; DE Short=PEL I; DE AltName: Full=Pectate lyase A; DE Short=PLA; DE Flags: Precursor; GN Name=pel1; Synonyms=pelA; OrderedLocusNames=ECA4067; OS Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=29471; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-36. RC STRAIN=EC; RX MEDLINE=88226011; 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 MEDLINE=95291436; PubMed=7773390; RA Bartling S., Wegener C., Olsen O.; RT "Synergism between Erwinia pectate lyase isoenzymes that depolymerize RT both 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 RT carotovora subsp. atroseptica and characterization of virulence RT 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: Eliminative cleavage of (1->4)-alpha-D- CC galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact- CC 4-enuronosyl groups at their non-reducing ends. CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity). CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy- CC D-gluconic acid from pectin: step 2/5. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLADES CC subfamily. 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; YP_052154.1; -. DR HSSP; P11073; 1AIR. DR GeneID; 2885350; -. DR GenomeReviews; BX950851_GR; ECA4067. DR KEGG; eca:ECA4067; -. DR NMPDR; fig|218491.3.peg.2898; -. DR HOGENOM; Q6CZT4; -. DR BioCyc; ECAR218491:ECA4067-MON; -. DR BRENDA; 4.2.2.2; 281579. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030570; F:pectate lyase activity; IEA:EC. DR InterPro; IPR002022; Amb_allergen. DR InterPro; IPR012334; Pectin_lyas_fold. DR Gene3D; G3DSA:2.160.20.10; Pectin_lyas_fold; 1. DR Pfam; PF00544; Pec_lyase_C; 1. DR SMART; SM00656; Amb_all; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Direct protein sequencing; Disulfide bond; KW Lyase; Metal-binding; Secreted; Signal. FT SIGNAL 1 22 FT CHAIN 23 374 Pectate lyase 1. FT /FTId=PRO_0000234448. FT ACT_SITE 239 239 Potential. FT METAL 150 150 Calcium (By similarity). FT METAL 152 152 Calcium (By similarity). FT METAL 187 187 Calcium (By similarity). FT METAL 191 191 Calcium (By similarity). FT DISULFID 93 176 By similarity. FT DISULFID 350 373 By similarity. FT CONFLICT 13 13 L -> V (in Ref. 2; CAA57439). FT CONFLICT 51 66 VDIIEAAKKDSSGKVV -> INLIEEAQLDSKGKKL (in FT Ref. 1; AA sequence). FT CONFLICT 65 65 V -> A (in Ref. 2; CAA57439). FT CONFLICT 71 71 F -> Y (in Ref. 1; AAA24845 and 2; FT CAA57439). FT CONFLICT 112 112 I -> L (in Ref. 1; AAA24845). FT CONFLICT 128 128 V -> L (in Ref. 1; AAA24845). FT CONFLICT 128 128 V -> M (in Ref. 2; CAA57439). FT CONFLICT 135 135 V -> I (in Ref. 2; CAA57439). FT CONFLICT 154 154 I -> V (in Ref. 1; AAA24845). FT CONFLICT 195 195 A -> G (in Ref. 1; AAA24845). FT CONFLICT 205 205 F -> Y (in Ref. 1; AAA24845 and 2; FT CAA57439). FT CONFLICT 228 228 Y -> H (in Ref. 1; AAA24845). FT CONFLICT 233 233 Y -> H (in Ref. 1; AAA24845). FT CONFLICT 252 252 N -> T (in Ref. 1; AAA24845). FT CONFLICT 256 256 D -> G (in Ref. 2; CAA57439). FT CONFLICT 314 314 K -> N (in Ref. 2; CAA57439). FT CONFLICT 340 340 S -> P (in Ref. 1; AAA24845 and 2; FT CAA57439). FT CONFLICT 357 357 N -> S (in Ref. 2; CAA57439). 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 //