ID R0GMC6_9BRAS Unreviewed; 374 AA. AC R0GMC6; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 04-FEB-2015, entry version 12. DE RecName: Full=Pectate lyase {ECO:0000256|RuleBase:RU361123}; DE EC=4.2.2.2 {ECO:0000256|RuleBase:RU361123}; GN ORFNames=CARUB_v10006459mg {ECO:0000313|EMBL:EOA18019.1}; OS Capsella rubella. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Capsella. OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA18019.1}; RN [1] {ECO:0000313|EMBL:EOA18019.1} RP NUCLEOTIDE SEQUENCE. RA Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., RA Wright S.; RT "Genome sequencing of Capsella rubella."; RL Nat. Genet. 0:0-0(2013). 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 {ECO:0000256|RuleBase:RU361123}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361123}; CC Note=Binds 1 Ca(2+) ion. Required for its activity. CC {ECO:0000256|RuleBase:RU361123}; CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy- CC D-gluconate from pectin: step 2/5. CC {ECO:0000256|RuleBase:RU361123}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. CC {ECO:0000256|RuleBase:RU361123}. 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; KB870811; EOA18019.1; -; Genomic_DNA. DR RefSeq; XP_006285121.1; XM_006285059.1. DR GeneID; 17878980; -. DR KEGG; crb:CARUB_v10006459mg; -. DR KO; K01728; -. DR UniPathway; UPA00545; UER00824. 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; Amb_allergen_dom. DR InterPro; IPR018082; AmbAllergen. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF00544; Pec_lyase_C; 1. DR PRINTS; PR00807; AMBALLERGEN. DR SMART; SM00656; Amb_all; 1. DR SUPFAM; SSF51126; SSF51126; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|RuleBase:RU361123}; KW Lyase {ECO:0000256|RuleBase:RU361123}; KW Metal-binding {ECO:0000256|RuleBase:RU361123}; KW Signal {ECO:0000256|RuleBase:RU361123}. FT SIGNAL 1 24 {ECO:0000256|RuleBase:RU361123}. FT CHAIN 25 374 Pectate lyase. {ECO:0000256|RuleBase: FT RU361123}. FT /FTId=PRO_5001354018. SQ SEQUENCE 374 AA; 40374 MW; DA7E8BB9FDDFFBCF CRC64; MDSLVITISL VFAILASLLV ESSAHNHSDD GYTLATATLN PIDACWRKNP KWSTNRQALA HCAVGFGKAA LGGKAGAIYV VTSPLDDPVK PKPGTLRFGV IQSKPLWITF ARSMVIVLKV ELSVNSYKTI DGRGAKVEIA NGPCVRMRLV KHVIIHGISI HDCKPGPKEG PDGDAIRVFQ SSHIWIDHCF LSRSQDGLID VISSSTAVTI SNNKFTNHDK VILLGHDDKF TGDKVMKVTV AFNYFGPGLI ERMPRVRRGY AHVANNRYDK WKMYAIGGSA DPIIFSEGNY FVAPDNKNAK EVTKRVGSAA EIKKWKWGTS KDVFLNGAFF VPSGGPAVKP AYAKGEAFPV APGSLVPSLT ASAGPLNCVV GKIC //