ID PLY19_ARATH Reviewed; 472 AA. AC Q9LFP5; A0MFG0; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 04-NOV-2026, entry version 155. DE RecName: Full=Probable pectate lyase 19; DE EC=4.2.2.2; DE Flags: Precursor; GN OrderedLocusNames=At5g15110; ORFNames=F2G14.230; 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=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., RA Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."; RL Nature 408:823-826(2000). RN [2] RP GENOME REANNOTATION, AND SEQUENCE REVISION. 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). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x; RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.; RT "Simultaneous high-throughput recombinational cloning of open reading RT frames in closed and open configurations."; RL Plant Biotechnol. J. 4:317-324(2006). 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=ABK28696.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL391146; CAC01830.1; -; Genomic_DNA. DR EMBL; CP002688; AED92118.1; -; Genomic_DNA. DR EMBL; OZ408687; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ653286; ABK28696.1; ALT_SEQ; mRNA. DR PIR; T51456; T51456. DR RefSeq; NP_197015.4; NM_121515.6. DR AlphaFoldDB; Q9LFP5; -. DR SMR; Q9LFP5; -. DR FunCoup; Q9LFP5; 107. DR STRING; 3702.Q9LFP5; -. DR GlyCosmos; Q9LFP5; 3 sites, No reported glycans. DR GlyGen; Q9LFP5; 3 sites. DR PaxDb; 3702-Q9LFP5; -. DR PeptideAtlas; Q9LFP5; -. DR ProteomicsDB; 234734; -. DR GeneID; 831363; -. DR KEGG; ath:AT5G15110; -. DR Araport; AT5G15110; -. DR TAIR; AT5G15110; -. DR eggNOG; ENOG502QQE2; Eukaryota. DR HOGENOM; CLU_026608_2_1_1; -. DR InParanoid; Q9LFP5; -. DR OMA; AETTYKH; -. DR PhylomeDB; Q9LFP5; -. DR BioCyc; ARA:AT5G15110-MONOMER; -. DR UniPathway; UPA00545; UER00824. DR PRO; PR:Q9LFP5; -. DR Proteomes; UP000006548; Chromosome 5. DR Proteomes; UP001984100; Chromosome 5. DR GO; GO:0005576; C:extracellular region; ISM:TAIR. DR GO; GO:0030570; F:pectate lyase activity; IBA:GO_Central. DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; PECTATE LYASE 18-RELATED; 1. DR PANTHER; PTHR31683:SF161; PECTATE LYASE 19-RELATED; 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; Pectin lyase-like; 1. PE 2: Evidence at transcript level; KW Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..472 FT /note="Probable pectate lyase 19" FT /id="PRO_0000024884" FT REGION 64..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..83 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 348 FT /evidence="ECO:0000255" FT BINDING 268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 292 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 296 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 66 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 97 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 237 FT /note="I -> V (in Ref. 2; AED92118 and 4; ABK28696)" FT /evidence="ECO:0000305" SQ SEQUENCE 472 AA; 53851 MW; E0D84351D7F57D75 CRC64; MEMVRLSKLM FTFCIAVLIP TIRGNISELD EYWSQRADEA REFTLQAYHS DPYEIVDHFH ERHYDNSTDV TTPEEDGDAK PEEEEKEFIE MLGSSTNSTR RSLRGKGKGK WSKLKGPCTA SNPIDKCWRC RSDWAKRRKK LTRCVRGFGH RTTGGKRGRI YVVTSNLDED MVNPKPGTLR HAVIQKEPLW IIFKNDMSIR LNQELLINSH KTIDARGANV HVAHGAGITM QFVKNVIIHG LHIHHISESS GGMIRDSVDH FGMRTRADGD GLSIYGSSNI WLDHISMSKC QDGLIDAIVG STGITISNSH FTHHNDVMLL GAQNTNEADK HMQVTVAYNH FGKGLVQRMP RIRWGFVHVV NNDYTHWELY AIGGSQGPTI LSHGNRFIAP PHKPHYREVT KRDYASEDEW KHWNWRSDKD VFMNGAYFRQ SGNPQYKCAH TRQQMIKPKN GLAVSKLTKY AGALDCRVGR RC //