ID A5CLY6_CLAM3 Unreviewed; 283 AA. AC A5CLY6; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 10-JUN-2026, entry version 73. DE RecName: Full=Pectate lyase {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009}; DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009}; GN Name=pelA2 {ECO:0000313|EMBL:CAN00065.1}; GN OrderedLocusNames=CMM_0051 {ECO:0000313|EMBL:CAN00065.1}; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Microbacteriaceae; Clavibacter. OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN00065.1, ECO:0000313|Proteomes:UP000001564}; RN [1] {ECO:0000313|EMBL:CAN00065.1, ECO:0000313|Proteomes:UP000001564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN00065.1, RC ECO:0000313|Proteomes:UP000001564}; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M., RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O., RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C., RA Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O., RA Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved RT in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). CC -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and CC pectins of methyl esterification degree from 22 to 89%, with an endo CC mode of action. In contrast to the majority of pectate lyases, displays CC high activity on highly methylated pectins. CC {ECO:0000256|RuleBase:RU367009}. 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 Evidence={ECO:0000256|ARBA:ARBA00000695, CC ECO:0000256|RuleBase:RU367009}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913, CC ECO:0000256|RuleBase:RU367009}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU367009}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family. CC {ECO:0000256|ARBA:ARBA00006463, ECO:0000256|RuleBase:RU367009}. 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; AM711867; CAN00065.1; -; Genomic_DNA. DR RefSeq; WP_011931270.1; NC_009480.1. DR AlphaFoldDB; A5CLY6; -. DR KEGG; cmi:CMM_0051; -. DR eggNOG; COG5297; Bacteria. DR HOGENOM; CLU_044863_3_1_11; -. DR OrthoDB; 4298856at2; -. DR Proteomes; UP000001564; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule. DR GO; GO:0045490; P:pectin catabolic process; IEA:TreeGrafter. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1. DR PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1. DR Pfam; PF03211; Pectate_lyase; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367009}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367009}; KW Reference proteome {ECO:0000313|Proteomes:UP000001564}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367009}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. SQ SEQUENCE 283 AA; 29388 MW; 3F573B37ACBDBB0D CRC64; MPPLLPARRH HLATRPWAVA LVVLIAIGGV AAVPASSAHA AGLPAQGSTI STLPAFPAPT SVKPPRATPY EVPAGQTVDY NNAELNGSTS GRGEFQQPVI LVHPGGTVKN VIIGPLAADG IHCEASCTIE NMYSSHVGED AVTLLDGSPT PSVVTIQGGG VQHAYDKVVQ MDGAGTVRIM HFAASDIGSL VRSCGNCPHQ YPRHIVVSDV FIDGGRYKVA GVNQNFGDTA KLDHITIRGT RMQVCDRTIG GRGTPAKEVP GGSGDPYAGV CDFSYATILF EHG //