ID   PLY2_AMBAR              Reviewed;         397 AA.
AC   P27761;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   22-FEB-2023, entry version 91.
DE   RecName: Full=Pectate lyase 2;
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 1.3;
DE   AltName: Allergen=Amb a 1.3;
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).
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; M62961; AAA32668.1; -; mRNA.
DR   EMBL; M80560; AAA32669.1; ALT_SEQ; mRNA.
DR   PIR; C39099; C39099.
DR   PIR; C53240; C53240.
DR   AlphaFoldDB; P27761; -.
DR   SMR; P27761; -.
DR   Allergome; 24; Amb a 1.
DR   Allergome; 789; Amb a 1.0301.
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; Single-stranded right-handed beta-helix, Pectin lyase-like; 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:SF159; PECTATE LYASE; 1.
DR   PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   PRINTS; PR00807; AMBALLERGEN.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 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..397
FT                   /note="Pectate lyase 2"
FT                   /id="PRO_0000024903"
FT   ACT_SITE        274
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         48
FT                   /note="L -> Y"
SQ   SEQUENCE   397 AA;  42928 MW;  C8DB41257590DD0A CRC64;
     MGIKQCCYIL YFTLALVALL QPVRSAEGVG EILPSVNETR SLQACEALNI IDKCWRGKAD
     WENNRQALAD CAQGFAKGTY GGKWGDVYTV TSNLDDDVAN PKEGTLRFAA AQNRPLWIIF
     KNDMVINLNQ ELVVNSDKTI DGRGVKVEII NGGLTLMNVK NIIIHNINIH DVKVLPGGMI
     KSNDGPPILR QASDGDTINV AGSSQIWIDH CSLSKSFDGL VDVTLGSTHV TISNCKFTQQ
     SKAILLGADD THVQDKGMLA TVAFNMFTDN VDQRMPRCRF GFFQVVNNNY DRWGTYAIGG
     SSAPTILCQG NRFLAPDDQI KKNVLARTGT GAAESMAWNW RSDKDLLENG AIFVTSGSDP
     VLTPVQSAGM IPAEPGEAAI KLTSSAGVFS CHPGAPC
//