ID   PLY_ZINVI               Reviewed;         401 AA.
AC   O24554;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Pectate lyase;
DE            EC=4.2.2.2;
DE   AltName: Full=ZePel;
DE   Flags: Precursor;
OS   Zinnia violacea (Garden zinnia) (Zinnia elegans).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Zinnia.
OX   NCBI_TaxID=34245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Envy;
RX   PubMed=9680962; DOI=10.1046/j.1365-313x.1998.00002.x;
RA   Domingo C., Roberts K., Stacey N.J., Connerton I., Ruiz-Teran F.,
RA   McCann M.C.;
RT   "A pectate lyase from Zinnia elegans is auxin inducible.";
RL   Plant J. 13:17-28(1998).
CC   -!- FUNCTION: Involved in the degradation of pectin. May assist in the
CC       removal and modification of an existing pectin matrix in order to allow
CC       the deposition of newly synthesized walls polymers for a specialized
CC       function or to create an architecture that is extensible.
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;
CC       Note=Binds 1 Ca(2+) ion. Required for its activity.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=0.12 umol/min/mg enzyme;
CC       pH dependence:
CC         Optimum pH is 10.;
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- TISSUE SPECIFICITY: Expressed in sites of vascular differentiation and
CC       in new primordia on the flank of the shoot meristem.
CC   -!- INDUCTION: Up-regulated by auxin.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; Y09541; CAA70735.1; -; mRNA.
DR   AlphaFoldDB; O24554; -.
DR   SMR; O24554; -.
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   Calcium; Glycoprotein; Lyase; Metal-binding; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..401
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024893"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000255"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   401 AA;  44407 MW;  B5EA3B57A9830F02 CRC64;
     MATTILPLIL FISSLAIASS SPSRTPHAIV NEVHKSINAS RRNLGYLSCG TGNPIDDCWR
     CDPNWANNRQ RLADCAIGFG KNAMGGRNGR IYVVTDPGND DPVNPVPGTL RYAVIQDEPL
     WIIFKRDMVI QLRQELVMNS HKTIDGRGVN VHIGNGPCIT IHYASNIIIH GIHIHDCKQA
     GNGNIRNSPH HSGWWTQSDG DGISIFASKD IWIDHNSLSN CHDGLIDAIH GSTAITISNN
     YMTHHDKVML LGHSDSYTQD KNMQVTIAFN HFGEGLVQRM PRCRHGYFHV VNNDYTHWEM
     YAIGGSASPT IYSQGNRFLA PNTRFDKEVT KHENAPESEW KNWNWRSEGD LMLNGAYFRE
     SGGRAASSFA RASSLSGRPS TLVASMTRSA GALVCRKGSR C