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}.
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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
//