ID   PLY21_ARATH             Reviewed;         392 AA.
AC   Q9FM66;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Putative pectate lyase 21;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g55720; ORFNames=MDF20.16;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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; AB009050; BAB09239.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96672.1; -; Genomic_DNA.
DR   RefSeq; NP_200383.1; NM_124954.3.
DR   AlphaFoldDB; Q9FM66; -.
DR   SMR; Q9FM66; -.
DR   STRING; 3702.AT5G55720.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; Q9FM66; -.
DR   PRIDE; Q9FM66; -.
DR   ProteomicsDB; 236570; -.
DR   EnsemblPlants; AT5G55720.1; AT5G55720.1; AT5G55720.
DR   GeneID; 835666; -.
DR   Gramene; AT5G55720.1; AT5G55720.1; AT5G55720.
DR   KEGG; ath:AT5G55720; -.
DR   Araport; AT5G55720; -.
DR   TAIR; locus:2162182; AT5G55720.
DR   eggNOG; ENOG502QS04; Eukaryota.
DR   HOGENOM; CLU_026608_0_1_1; -.
DR   InParanoid; Q9FM66; -.
DR   OMA; GWEMYAI; -.
DR   OrthoDB; 924221at2759; -.
DR   PhylomeDB; Q9FM66; -.
DR   BioCyc; ARA:AT5G55720-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:Q9FM66; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FM66; baseline and differential.
DR   Genevisible; Q9FM66; AT.
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   3: Inferred from homology;
KW   Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..392
FT                   /note="Putative pectate lyase 21"
FT                   /id="PRO_0000024886"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000255"
FT   BINDING         189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
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   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   392 AA;  43682 MW;  305F94A437C30ECB CRC64;
     MSIVCTFFLF LLNTSFAFAF AIPKPPIVRR LSTTVTSNST ASSCSANGNP IDECWRCDEN
     WKDNRKNLAD CAVGFGRDSI GGRAGEFYTV TDSGDDNPLN PTPGTLRYAA TQDQPLWIIF
     DRDMVIQLKQ DLQVASYKTI DGRGNNVQIA YGPCLTLYKV SNIIINNLYI HDCVPVKRNA
     LSSLGGYSDG DGISIFESRD IWIDHCTLEK CYDGLIDAVN GSTDITISNS YMLNHNEVML
     LGHSDEYSGD RDMRVTIAFN YFGEGLVQRM PRCRHGYFHI VNNIYRDWKM YAIGGSANPT
     IFSQGNVFIA SNNQFTKEVT KRESADGDEE WKEWNWKSEG DEMVNGAFFT PSGKEDSPSY
     AKFSSMVARP ASLLKTTHPS VGVLSCEIDQ AC