ID   R0GMC6_9BRAS            Unreviewed;       374 AA.
AC   R0GMC6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   29-SEP-2021, entry version 32.
DE   RecName: Full=Pectate lyase {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU361123};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU361123};
GN   ORFNames=CARUB_v10006459mg {ECO:0000313|EMBL:EOA18019.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Wright S.;
RT   "Genome sequencing of Capsella rubella.";
RL   Nat. Genet. 0:0-0(2013).
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: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-D-
CC       gluconate from pectin: step 2/5. {ECO:0000256|ARBA:ARBA00005220,
CC       ECO:0000256|RuleBase:RU361123}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010980, ECO:0000256|RuleBase:RU361123}.
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DR   EMBL; KB870811; EOA18019.1; -; Genomic_DNA.
DR   RefSeq; XP_006285121.1; XM_006285059.1.
DR   STRING; 81985.XP_006285121.1; -.
DR   GeneID; 17878980; -.
DR   KEGG; crb:17878980; -.
DR   eggNOG; ENOG502QSYA; Eukaryota.
DR   OrthoDB; 924221at2759; -.
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; IPR018082; AmbAllergen.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00544; Pectate_lyase_4; 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|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361123};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361123};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361123}; Signal {ECO:0000256|RuleBase:RU361123}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU361123"
FT   CHAIN           25..374
FT                   /note="Pectate lyase"
FT                   /evidence="ECO:0000256|RuleBase:RU361123"
FT                   /id="PRO_5005145123"
FT   DOMAIN          113..297
FT                   /note="Amb_all"
FT                   /evidence="ECO:0000259|SMART:SM00656"
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
//