ID   PLY56_SOLLC             Reviewed;         398 AA.
AC   P15721;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable pectate lyase P56;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=LAT56;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. VF36; TISSUE=Anther;
RX   PubMed=1983191; DOI=10.1007/bf00015651;
RA   Wing R.A., Yamaguchi J., Larabell S.K., Ursin V.M., McCormick S.;
RT   "Molecular and genetic characterization of two pollen-expressed genes that
RT   have sequence similarity to pectate lyases of the plant pathogen Erwinia.";
RL   Plant Mol. Biol. 14:17-28(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Wing R.A.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Might be needed during pollen development and tube growth.
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   -!- TISSUE SPECIFICITY: Expressed in anthers and pollen.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; X15500; CAA33524.1; -; Genomic_DNA.
DR   PIR; T07058; T07058.
DR   RefSeq; NP_001296315.1; NM_001309386.1.
DR   AlphaFoldDB; P15721; -.
DR   SMR; P15721; -.
DR   STRING; 4081.Solyc03g058910.2.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; P15721; -.
DR   PRIDE; P15721; -.
DR   EnsemblPlants; Solyc03g058910.3.1; Solyc03g058910.3.1; Solyc03g058910.3.
DR   GeneID; 101253756; -.
DR   Gramene; Solyc03g058910.3.1; Solyc03g058910.3.1; Solyc03g058910.3.
DR   KEGG; sly:101253756; -.
DR   eggNOG; ENOG502QQE2; Eukaryota.
DR   HOGENOM; CLU_026608_2_1_1; -.
DR   InParanoid; P15721; -.
DR   OMA; LFGANDH; -.
DR   OrthoDB; 924221at2759; -.
DR   PhylomeDB; P15721; -.
DR   UniPathway; UPA00545; UER00824.
DR   Proteomes; UP000004994; Chromosome 3.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..398
FT                   /note="Probable pectate lyase P56"
FT                   /id="PRO_0000024890"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000255"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   398 AA;  44564 MW;  8D676250BD8BC7C8 CRC64;
     MEYSYRTKIN VLFIVLILFV FAALGTAINA PRRKLTKKYR GPCMAVNSID KCWRCDPFWA
     EDRQKMADCA LGFGINAMGG KYGPYYIVTD NSDDDVVDPK PGTLRFGVIQ KGPLWITFAR
     SMRIRLTREL IVSSNKTIDG RGKYVHIANG AGIKIQSASN VIISNLRIHN IVPTAGGLLR
     ESDDHLGLRG ADEGDAISIF NSHDIWIDHI SMSRATDGLI DAVAGSTNIT ISNCHFTDHE
     KVMLFGANDH AEEDRGMKIT LAYNHFGKRL DQRMPRCRFG FFHLVNNDYT HWERYAIGGS
     SGATIISQGN RFIAEDKLLV KEVTYREKST SSVEEWMKWT WITDGDDFEN GATFTPSGDQ
     NLLSKIDHLN LIQPEPSSKV GLLTKFSGAL SCKIRRPC