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 02-SEP-2026, entry version 77. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 BRENDA; 4.2.2.2; 8352. DR UniPathway; UPA00545; UER00824. 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:SF80; PECTATE LYASE 16-RELATED; 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..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 //