ID   PLY_LILLO               Reviewed;         434 AA.
AC   P40973;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 90.
DE   RecName: Full=Pectate lyase;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
OS   Lilium longiflorum (Trumpet lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX   NCBI_TaxID=4690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nellie white; TISSUE=Pollen;
RA   Kim S.R., Finkel D.J., An G.;
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
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. Required for its activity. {ECO:0000250};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z17328; CAA78976.1; -; mRNA.
DR   EMBL; L18911; AAA33398.1; -; mRNA.
DR   PIR; S29612; S29612.
DR   AlphaFoldDB; P40973; -.
DR   SMR; P40973; -.
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; IPR007524; Pec_lyase_N.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683:SF208; PECTATE LYASE; 1.
DR   PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR   Pfam; PF04431; Pec_lyase_N; 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   2: Evidence at transcript level;
KW   Calcium; Glycoprotein; Lyase; Metal-binding; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..434
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024888"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   434 AA;  48457 MW;  C1F3E30AD2BBD064 CRC64;
     MKAAQFFLYS LLFFASAALS SANIAEFDEY WQKKSKVAQA KAKKAYTPHP EEVTNHFNKA
     VHSSFEGNST RRNLRTNKLG QCLATNPIDR CWRCKKNWSA NRKDLVKCVK GFGRKTTGGA
     AGEIYVVTDP SDDSLTDPKF GTLRWGVIQD RPLWIIFGKS MVIRLKQELI INNDKTIDGR
     GANVQIAGGA QLTVQFVHNV IIHGIHIHDI KPGEGGLIRD SEKHSGIRTR SDGDGISIIG
     SSNIWIDHVS LARCSDGLID VILGSTAITI SNCHLTEHDD VMLLGASDTY TQDEIMQVTV
     AFNHFGRGLV QRMPRCRYGF VHVVNNDYTH WIMYAVGGSQ HPTIISQGNR YIAPHIEAAK
     EVTKRDYAEP AEWSKWTWKS QGDLFVSGAF FVESGGPFEN KYSKKDLIKA KPGTFVQRLT
     RFSGALNCKE NMEC
//