PLY1_HESAR
ID PLY1_HESAR Reviewed; 367 AA.
AC Q9SCG9; A0T2M2; Q93XL6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Pectate lyase 1;
DE EC=4.2.2.2;
DE AltName: Full=Major pollen allergen Cup a 1;
DE AltName: Allergen=Cup a 1;
DE Flags: Precursor;
OS Hesperocyparis arizonica (Arizona cypress) (Cupressus arizonica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Hesperocyparis.
OX NCBI_TaxID=49011;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pollen;
RA Butteroni C., Di Felice G., Pini C.;
RT "Cloning of Cupressus Arizonica major allergen.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-367.
RC TISSUE=Pollen;
RX PubMed=19902388; DOI=10.1007/s12033-009-9219-z;
RA Pico de Coana Y., Parody N., Fernandez-Caldas E., Alonso C.;
RT "A modified protocol for RNA isolation from high polysaccharide containing
RT Cupressus arizonica pollen. Applications for RT-PCR and phage display
RT library construction.";
RL Mol. Biotechnol. 44:127-132(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-367, AND ALLERGEN.
RX PubMed=11122214; DOI=10.1046/j.1365-2222.2000.00949.x;
RA Aceituno E., Del Pozo V., Minguez A., Arrieta I., Cortegano I., Cardaba B.,
RA Gallardo S., Rojo M., Palomino P., Lahoz C.;
RT "Molecular cloning of major allergen from Cupressus arizonica pollen: Cup a
RT 1.";
RL Clin. Exp. Allergy 30:1750-1758(2000).
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 -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:11122214}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ278498; CAC37790.2; -; mRNA.
DR EMBL; EF079863; ABK78766.1; -; mRNA.
DR EMBL; AJ243570; CAB62551.1; -; mRNA.
DR AlphaFoldDB; Q9SCG9; -.
DR SMR; Q9SCG9; -.
DR Allergome; 256; Cup a 1.
DR Allergome; 3232; Cup a 1.0101.
DR Allergome; 895; Cup a 1.02.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..367
FT /note="Pectate lyase 1"
FT /id="PRO_0000212997"
FT ACT_SITE 250
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..45
FT /evidence="ECO:0000250"
FT DISULFID 128..147
FT /evidence="ECO:0000250"
FT DISULFID 306..312
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="S -> L (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> D (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="A -> N (in Ref. 2; ABK78766)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="D -> V (in Ref. 3; CAB62551)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> T (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="K -> I (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="N -> S (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="T -> S (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> F (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> E (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> T (in Ref. 1; CAC37790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 39776 MW; 0138EE8653B1ABDB CRC64;
MASPCLVAVL VFLCAIVSCY SDNPIDSCWR GDSNWDQNRM KLADCVVGFG SSTMGGKGGE
IYTVTSSEDN PVNPTPGTLR YGATREKALW IIFSQNMNIK LQMPLYVAGY KTIDGRGADV
HLGNGGPCLF MRKASHVILH GLHIHGCNTS VLGDVLVSES IGVEPVHAQD GDAITMRNVT
NAWIDHNSLS DCSDGLIDVT LGSTGITISN NHFFNHHKVM LLGHDDTYDD DKSMKVTVAF
NQFGPNAGQR MPRARYGLVH VANNNYDQWN IYAIGGSSNP TILSEGNSFT APNESYKKEV
TKRIGCETTS ACANWVWRST RDAFTNGAYF VSSGKAEDTN IYNSNEAFKV ENGNAAPQLT
QNAGVVA
