ID   PLY1_AMBAR              Reviewed;         398 AA.
AC   P27760; Q9S8F7;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Pectate lyase 1;
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 1.2;
DE   AltName: Full=Protein AaBA;
DE   AltName: Allergen=Amb a 1.2;
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 ALLERGEN.
RC   TISSUE=Pollen;
RX   PubMed=1702434; DOI=10.1016/s0021-9258(17)35305-x;
RA   Rafnar T., Griffith I.J., Kuo M.-C., Bond J.F., Rogers B.L., Klapper D.G.;
RT   "Cloning of Amb a I (antigen E), the major allergen family of short ragweed
RT   pollen.";
RL   J. Biol. Chem. 266:1229-1236(1991).
RN   [2]
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 44-69.
RX   PubMed=7783755; DOI=10.1016/0161-5890(95)00014-6;
RA   Pilyavskaya A., Wieczorek M., Jones S.W., Gross K.;
RT   "Isolation and characterization of a new basic antigen from short ragweed
RT   pollen (Ambrosia artemisiifolia).";
RL   Mol. Immunol. 32:523-529(1995).
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. {ECO:0000269|PubMed:1702434}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M62981; AAA32666.1; -; mRNA.
DR   EMBL; M80559; AAA32667.1; -; mRNA.
DR   PIR; B39099; B39099.
DR   PIR; B53240; B53240.
DR   AlphaFoldDB; P27760; -.
DR   SMR; P27760; -.
DR   Allergome; 24; Amb a 1.
DR   Allergome; 788; Amb a 1.0201.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PRIDE; P27760; -.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Lyase; Metal-binding; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..398
FT                   /note="Pectate lyase 1"
FT                   /id="PRO_0000024902"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000255"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
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        55..72
FT                   /evidence="ECO:0000250"
FT   VARIANT         345
FT                   /note="R -> K"
FT   VARIANT         381
FT                   /note="L -> I"
SQ   SEQUENCE   398 AA;  43665 MW;  020DC662D9B7416C CRC64;
     MGIKHCCYIL YFTLALVTLL QPVRSAEDVE EFLPSANETR RSLKACEAHN IIDKCWRCKA
     DWANNRQALA DCAQGFAKGT YGGKHGDVYT VTSDKDDDVA NPKEGTLRFA AAQNRPLWII
     FKRNMVIHLN QELVVNSDKT IDGRGVKVNI VNAGLTLMNV KNIIIHNINI HDIKVCPGGM
     IKSNDGPPIL RQQSDGDAIN VAGSSQIWID HCSLSKASDG LLDITLGSSH VTVSNCKFTQ
     HQFVLLLGAD DTHYQDKGML ATVAFNMFTD HVDQRMPRCR FGFFQVVNNN YDRWGTYAIG
     GSSAPTILSQ GNRFFAPDDI IKKNVLARTG TGNAESMSWN WRTDRDLLEN GAIFLPSGSD
     PVLTPEQKAG MIPAEPGEAV LRLTSSAGVL SCHQGAPC