PLY19_ARATH
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 03-AUG-2022, entry version 141.
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 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};
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DR EMBL; AL391146; CAC01830.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92118.1; -; 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 STRING; 3702.AT5G15110.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q9LFP5; -.
DR PeptideAtlas; Q9LFP5; -.
DR PRIDE; Q9LFP5; -.
DR ProteomicsDB; 234734; -.
DR GeneID; 831363; -.
DR KEGG; ath:AT5G15110; -.
DR Araport; AT5G15110; -.
DR eggNOG; ENOG502QQE2; Eukaryota.
DR HOGENOM; CLU_026608_2_1_1; -.
DR InParanoid; Q9LFP5; -.
DR OrthoDB; 924221at2759; -.
DR PhylomeDB; Q9LFP5; -.
DR BioCyc; ARA:AT5G15110-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q9LFP5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFP5; baseline and differential.
DR Genevisible; Q9LFP5; 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; 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..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 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 3; 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
