ID   PLY_TOBAC               Reviewed;         397 AA.
AC   P40972;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Pectate lyase;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Samsun; TISSUE=Pollen;
RX   PubMed=1421152; DOI=10.1007/bf00040608;
RA   Rogers H.J., Harvey A., Lonsdale D.M.;
RT   "Isolation and characterization of a tobacco gene with homology to pectate
RT   lyase which is specifically expressed during microsporogenesis.";
RL   Plant Mol. Biol. 20:493-502(1992).
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   -!- DEVELOPMENTAL STAGE: Maximally expressed late in pollen development.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; X67158; CAA47630.1; -; Genomic_DNA.
DR   EMBL; X67159; CAA47631.1; -; mRNA.
DR   EMBL; X61102; CAA43414.1; -; Genomic_DNA.
DR   PIR; S26211; S26211.
DR   RefSeq; XP_016483544.1; XM_016628058.1.
DR   AlphaFoldDB; P40972; -.
DR   SMR; P40972; -.
DR   STRING; 4097.P40972; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PRIDE; P40972; -.
DR   GeneID; 107804209; -.
DR   KEGG; nta:107804209; -.
DR   OMA; LFGANDH; -.
DR   OrthoDB; 924221at2759; -.
DR   UniPathway; UPA00545; UER00824.
DR   Proteomes; UP000084051; Unplaced.
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   2: Evidence at transcript level;
KW   Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..397
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024892"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000255"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        156
FT                   /note="S -> C (in Ref. 1; CAA47631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189..190
FT                   /note="GS -> SG (in Ref. 1; CAA47631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200..202
FT                   /note="SSH -> DSR (in Ref. 1; CAA47631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="H -> N (in Ref. 1; CAA47631)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  44352 MW;  EF0A82CE5DA7643F CRC64;
     MDVYRIRISV FFLLVLLTFA ALTTATNIPR RQLSNKKYKG PCRAENAIDK CWRCDPNWAE
     NRQKMADCAL GFGSNAIGGK LGRIYVVTDN SDDDVVDPKP GTLRYGVIQK EPLWIIFGKN
     MKIKLSRELI VTSNKTIDGR GFNVHIQNGA GIKIQSASNI IISNLRIHNI VPTPGGLLRE
     SEDHVGLRGS DEGDGISIFS SHDIWIDHIS MSRATDGLID AVAASTNITI SNCHFTDHEK
     VMLFGANDHY VLDKDMKITL AYNHFGKRLD QRMPRCRFGF FHLVNNDYTH WERYAIGGSS
     GATIISQGNR FIAEDELLVK EVTYREKLTA SVAEWMKWTW ISDGDDMENG ATFTPSGDQN
     LLDKIDHLNL IKPEPSSKVG ILTKFSGALS CVKGRPC