PLY1_CHAOB
ID PLY1_CHAOB Reviewed; 375 AA.
AC Q96385;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Pectate lyase 1;
DE EC=4.2.2.2;
DE AltName: Full=Major pollen allergen Cha o 1;
DE AltName: Allergen=Cha o 1;
DE Flags: Precursor;
OS Chamaecyparis obtusa (Hinoki false-cypress) (Retinospora obtusa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Chamaecyparis.
OX NCBI_TaxID=13415;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=8676896; DOI=10.1016/0161-5890(95)00147-6;
RA Suzuki M., Komiyama N., Itoh M., Itoh H., Sone T., Kuno K., Takagi I.,
RA Ohta N.;
RT "Purification, characterization and molecular cloning of Cha o 1, a major
RT allergen of Chamaecyparis obtusa (Japanese cypress) pollen.";
RL Mol. Immunol. 33:451-460(1996).
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:8676896}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC subfamily. {ECO:0000305}.
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DR EMBL; D45404; BAA08246.1; -; mRNA.
DR AlphaFoldDB; Q96385; -.
DR SMR; Q96385; -.
DR Allergome; 197; Cha o 1.
DR Allergome; 3186; Cha o 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..21
FT CHAIN 22..375
FT /note="Pectate lyase 1"
FT /id="PRO_0000024907"
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 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 CARBOHYD 352
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"
SQ SEQUENCE 375 AA; 40258 MW; 81CD91DF7066DBBF CRC64;
MASCTLLAVL VFLCAIVSCF SDNPIDSCWR GDANWDQNRM KLADCAVGFG SSAMGGKGGA
FYTVTSSDDD PVNPAPGTLR YGATRERSLW IIFSKNLNIK LNMPLYIAGN KTIDGRGAEV
HIGNGGPCLF MRTVSHVILH GLNIHGCNTS VSGNVLISEA SGVVPVHAQD GDAITMRNVT
DVWIDHNSLS DSSDGLVDVT LASTGVTISN NHFFNHHKVM LLGHSDIYSD DKSMKVTVAF
NQFGPNAGQR MPRARYGLIH VANNNYDPWS IYAIGGSSNP TILSEGNSFT APNDSDKKEV
TRRVGCESPS TCANWVWRST QDSFNNGAYF VSSGKNEGTN IYNNNEAFKV ENGSAAPQLT
KNAGVLTCIL SKPCS
