ID   PLY3_AMBAR              Reviewed;         392 AA.
AC   P28744;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Pectate lyase 3;
DE            EC=4.2.2.2;
DE   AltName: Full=Antigen Amb a I;
DE   AltName: Full=Antigen E;
DE            Short=AgE;
DE   AltName: Full=Pollen allergen Amb a 1.4;
DE   AltName: Allergen=Amb a 1.4;
DE   Flags: Precursor;
OS   Ambrosia artemisiifolia (Common ragweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Ambrosia.
OX   NCBI_TaxID=4212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS.
RC   TISSUE=Pollen;
RX   PubMed=1809687; DOI=10.1159/000235512;
RA   Griffith I.J., Pollock J., Klapper D.G., Rogers B.L., Nault A.K.;
RT   "Sequence polymorphism of Amb a I and Amb a II, the major allergens in
RT   Ambrosia artemisiifolia (short ragweed).";
RL   Int. Arch. Allergy Appl. Immunol. 96:296-304(1991).
CC   -!- FUNCTION: Has pectate lyase activity. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Pollen and flowers.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- ALLERGEN: Causes an allergic reaction in human. This is one of the
CC       major allergens of the ragweed pollen.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M80562; AAA32670.1; -; mRNA.
DR   PIR; D53240; D53240.
DR   AlphaFoldDB; P28744; -.
DR   SMR; P28744; -.
DR   Allergome; 24; Amb a 1.
DR   Allergome; 790; Amb a 1.0401.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
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   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   PRINTS; PR00807; AMBALLERGEN.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Allergen; Calcium; Disulfide bond; Glycoprotein; Lyase; Metal-binding;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..392
FT                   /note="Pectate lyase 3"
FT                   /id="PRO_0000024904"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000255"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..71
FT                   /evidence="ECO:0000250"
FT   VARIANT         182..188
FT                   /note="SHDGPPV -> CNDGPPA"
SQ   SEQUENCE   392 AA;  42843 MW;  7B6219C12F365DA9 CRC64;
     MGIKHCCYIL YFTLALVTLL QPVRSAEDLQ QILPSANETR SLTTCGTYNI IDGCWRGKAD
     WAENRKALAD CAQGFAKGTI GGKDGDIYTV TSELDDDVAN PKEGTLRFGA AQNRPLWIIF
     ARDMVIRLDR ELAINNDKTI DGRGAKVEII NAGFAIYNVK NIIIHNIIMH DIVVNPGGLI
     KSHDGPPVPR KGSDGDAIGI SGGSQIWIDH CSLSKAVDGL IDAKHGSTHF TVSNCLFTQH
     QYLLLFWDFD ERGMLCTVAF NKFTDNVDQR MPNLRHGFVQ VVNNNYERWG SYALGGSAGP
     TILSQGNRFL ASDIKKEVVG RYGESAMSES INWNWRSYMD VFENGAIFVP SGVDPVLTPE
     QNAGMIPAEP GEAVLRLTSS AGVLSCQPGA PC