ID   PLY4_AMBAR              Reviewed;         397 AA.
AC   P27762;
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 4;
DE            EC=4.2.2.2;
DE   AltName: Full=Antigen Amb a II;
DE   AltName: Full=Antigen K;
DE            Short=AgK;
DE   AltName: Full=Pollen allergen Amb a 2;
DE   AltName: Allergen=Amb a 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=Flower;
RX   PubMed=1717566;
RA   Rogers B.L., Morgenstern J.P., Griffith I.J., Yu X.-B., Counsell C.M.,
RA   Brauer A.W., King T.P., Garman R.D., Kuo M.-C.C.;
RT   "Complete sequence of the allergen Amb alpha II. Recombinant expression and
RT   reactivity with T cells from ragweed allergic patients.";
RL   J. Immunol. 147:2547-2552(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:1717566}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M80561; AAA32671.1; -; mRNA.
DR   PIR; E53240; E53240.
DR   AlphaFoldDB; P27762; -.
DR   SMR; P27762; -.
DR   Allergome; 26; Amb a 1.0501.
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; IPR006626; PbH1.
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   SMART; SM00710; PbH1; 3.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   1: Evidence at protein level;
KW   Allergen; Calcium; Disulfide bond; Glycoprotein; Lyase; Metal-binding;
KW   Repeat; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..397
FT                   /note="Pectate lyase 4"
FT                   /id="PRO_0000024905"
FT   REPEAT          159..202
FT                   /note="PbH1 1"
FT   REPEAT          203..224
FT                   /note="PbH1 2"
FT   REPEAT          227..248
FT                   /note="PbH1 3"
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        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..71
FT                   /evidence="ECO:0000250"
FT   VARIANT         70
FT                   /note="N -> D (detected only in flower DNA)"
FT   VARIANT         138
FT                   /note="K -> T (detected only in flower DNA)"
FT   VARIANT         321
FT                   /note="K -> R (detected only in flower DNA)"
SQ   SEQUENCE   397 AA;  44082 MW;  C78617E4C9A3D1DD CRC64;
     MGIKHCCYIL YFTLALVTLV QAGRLGEEVD ILPSPNDTRR SLQGCEAHNI IDKCWRCKPD
     WAENRQALGN CAQGFGKATH GGKWGDIYMV TSDQDDDVVN PKEGTLRFGA TQDRPLWIIF
     QRDMIIYLQQ EMVVTSDKTI DGRGAKVELV YGGITLMNVK NVIIHNIDIH DVRVLPGGRI
     KSNGGPAIPR HQSDGDAIHV TGSSDIWIDH CTLSKSFDGL VDVNWGSTGV TISNCKFTHH
     EKAVLLGASD THFQDLKMHV TLAYNIFTNT VHERMPRCRF GFFQIVNNFY DRWDKYAIGG
     SSNPTILSQG NKFVAPDFIY KKNVCLRTGA QEPEWMTWNW RTQNDVLENG AIFVASGSDP
     VLTAEQNAGM MQAEPGDMVP QLTMNAGVLT CSPGAPC
//