PLY5_AMBAR
ID PLY5_AMBAR Reviewed; 396 AA.
AC P27759;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Pectate lyase 5;
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 1.1;
DE AltName: Allergen=Amb a 1.1;
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], PARTIAL PROTEIN SEQUENCE, 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 256-273 AND 292-306, AND ALLERGEN.
RX PubMed=2456454; DOI=10.1016/0161-5890(88)90030-2;
RA Smith J.J., Olson J.R., Klapper D.G.;
RT "Monoclonal antibodies to denatured ragweed pollen allergen Amb a I:
RT characterization, specificity for the denatured allergen, and utilization
RT for the isolation of immunogenic peptides of Amb a I.";
RL Mol. Immunol. 25:355-365(1988).
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 ECO:0000269|PubMed:2456454}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC subfamily. {ECO:0000305}.
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DR EMBL; M63116; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M80558; AAA32665.1; -; mRNA.
DR PIR; A39099; A39099.
DR AlphaFoldDB; P27759; -.
DR SMR; P27759; -.
DR Allergome; 24; Amb a 1.
DR Allergome; 787; Amb a 1.0101.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lyase; Metal-binding; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..396
FT /note="Pectate lyase 5"
FT /id="PRO_0000024901"
FT ACT_SITE 273
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 221
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 53..70
FT /evidence="ECO:0000250"
FT VARIANT 92
FT /note="E -> D"
FT CONFLICT 304
FT /note="T -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42709 MW; 0CE7DDECB2B8841D CRC64;
MGIKHCCYIL YFTLALVTLL QPVRSAEDLQ EILPVNETRR LTTSGAYNII DGCWRGKADW
AENRKALADC AQGFGKGTVG GKDGDIYTVT SELDDDVANP KEGTLRFGAA QNRPLWIIFE
RDMVIRLDKE MVVNSDKTID GRGAKVEIIN AGFTLNGVKN VIIHNINMHD VKVNPGGLIK
SNDGPAAPRA GSDGDAISIS GSSQIWIDHC SLSKSVDGLV DAKLGTTRLT VSNSLFTQHQ
FVLLFGAGDE NIEDRGMLAT VAFNTFTDNV DQRMPRCRHG FFQVVNNNYD KWGSYAIGGS
ASPTILSQGN RFCAPDERSK KNVLGRHGEA AAESMKWNWR TNKDVLENGA IFVASGVDPV
LTPEQSAGMI PAEPGESALS LTSSAGVLSC QPGAPC
