ID   PLY11_ARATH             Reviewed;         412 AA.
AC   Q9LTZ0; F4IWH8;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Putative pectate lyase 11;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g27400; ORFNames=K1G2.11;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA95715.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB024028; BAA95715.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77312.1; -; Genomic_DNA.
DR   RefSeq; NP_189376.1; NM_113655.2.
DR   AlphaFoldDB; Q9LTZ0; -.
DR   SMR; Q9LTZ0; -.
DR   STRING; 3702.AT3G27400.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; Q9LTZ0; -.
DR   PRIDE; Q9LTZ0; -.
DR   ProteomicsDB; 236577; -.
DR   EnsemblPlants; AT3G27400.1; AT3G27400.1; AT3G27400.
DR   GeneID; 822361; -.
DR   Gramene; AT3G27400.1; AT3G27400.1; AT3G27400.
DR   KEGG; ath:AT3G27400; -.
DR   Araport; AT3G27400; -.
DR   TAIR; locus:2086656; AT3G27400.
DR   eggNOG; ENOG502QVCJ; Eukaryota.
DR   HOGENOM; CLU_026608_0_1_1; -.
DR   InParanoid; Q9LTZ0; -.
DR   OMA; IHYETNI; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:Q9LTZ0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LTZ0; baseline and differential.
DR   Genevisible; Q9LTZ0; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
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   GO; GO:0009624; P:response to nematode; IMP:TAIR.
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; Lyase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..412
FT                   /note="Putative pectate lyase 11"
FT                   /id="PRO_0000024875"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000255"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  45985 MW;  4DBECAAFD83D2FB8 CRC64;
     MVSYSNNHFA YAFLLLLTIG NTLAFSSSLP DHVQDPNLVV DDVNRSVFNA SRRSLAYLSC
     RTGNPIDDCW RCDPNWETNR QRLADCAIGF GKNAIGGRKG RIYVVTDPAN DDPVNPRPGT
     LRYAVTQEEP LWIIFKRDMV IRLKKELIIT SFKTIDGRGS SVHITDGPCL KIHYATNIII
     HGINIHDCKP GSGGMIKDGP HHTGWWMQSD GDAVAIFGGK HVWIDHCSLS NCDDGLIDAI
     HGSTAITISN NHMTHHDKVM LLGHSDSYTQ DKNMQVTIAF NHFGEGLVQR MPRCRHGYFH
     VVNNDYTHWE MYAIGGSASP TIYSQGNRFL APNTRFNKEV TKHEDAPESK WRDWNWRSEG
     DMLLNGAYFR ESGAEAPSTY ARASSLSARP SSLVGSITTT AGTLSCRRGR RC