ID   PLY59_SOLLC             Reviewed;         449 AA.
AC   P15722;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable pectate lyase P59;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=LAT59;
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).
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; X15499; CAA33523.1; -; Genomic_DNA.
DR   PIR; S27098; S27098.
DR   AlphaFoldDB; P15722; -.
DR   SMR; P15722; -.
DR   STRING; 4081.Solyc03g058890.2.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; P15722; -.
DR   PRIDE; P15722; -.
DR   eggNOG; ENOG502QQE2; Eukaryota.
DR   InParanoid; P15722; -.
DR   UniPathway; UPA00545; UER00824.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P15722; baseline.
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; IPR007524; Pec_lyase_N.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 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; SSF51126; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..449
FT                   /note="Probable pectate lyase P59"
FT                   /id="PRO_0000024891"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000255"
FT   BINDING         245
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   449 AA;  50893 MW;  17E3AA13F173B03C CRC64;
     MGGPKIKYSF LFLCITFATI IPSLMAHIGH YDEVWRRRAE EAKEYARNIY EPHPENVTLA
     FNQKLRDTMK ELKKVKGTHN NSTRRGLGTK KYTGPCMVTN PIDKCWRCDP NWADNRKKLA
     DCAMGFGSKA IGGKDGEFYV VTDNSDDYND PKPGTLRHAV IQKEPLWIIF KRGMNIRLHQ
     EMIMQSDKTI DARGVNVHIT KGAGITLQYI KNVIIHGLHI HDIVEGNGGM VRDAVDHIGI
     RTKSDGDGIS IFGASYIWID HVSMQRCYDG LIDAVEGSTG ITISNGHFTD HNEVMLFGAS
     DSSSIDQVMQ ITLAFNHFGK RLIQRMPRCR WGYIHVVNND YTHWNMYAIG GSMHPTIIHQ
     GNRFIAPPDI FKKQVTKREY NPESVWMQWT WRSEGNLFMN GAYFTESGDP EWSSKHKDLY
     DGISAAPAED VTWMTRFAGV LGCKPGKPC