PLY22_ARATH
ID PLY22_ARATH Reviewed; 432 AA.
AC Q93Z25; Q9FMK5;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable pectate lyase 22;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN OrderedLocusNames=At5g63180; ORFNames=MDC12_15;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=BAB10560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB008265; BAB10560.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED97715.1; -; Genomic_DNA.
DR EMBL; AY058197; AAL25610.1; -; mRNA.
DR RefSeq; NP_568967.1; NM_125713.3.
DR AlphaFoldDB; Q93Z25; -.
DR SMR; Q93Z25; -.
DR STRING; 3702.AT5G63180.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q93Z25; -.
DR PRIDE; Q93Z25; -.
DR ProteomicsDB; 234676; -.
DR EnsemblPlants; AT5G63180.1; AT5G63180.1; AT5G63180.
DR GeneID; 836439; -.
DR Gramene; AT5G63180.1; AT5G63180.1; AT5G63180.
DR KEGG; ath:AT5G63180; -.
DR Araport; AT5G63180; -.
DR TAIR; locus:2161992; AT5G63180.
DR eggNOG; ENOG502QQ5F; Eukaryota.
DR HOGENOM; CLU_026608_0_1_1; -.
DR InParanoid; Q93Z25; -.
DR OMA; CKRGSHC; -.
DR OrthoDB; 924221at2759; -.
DR PhylomeDB; Q93Z25; -.
DR BioCyc; ARA:AT5G63180-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q93Z25; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93Z25; baseline and differential.
DR Genevisible; Q93Z25; AT.
DR GO; GO:0009536; C:plastid; 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 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 2: Evidence at transcript level;
KW Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..432
FT /note="Probable pectate lyase 22"
FT /id="PRO_0000024887"
FT ACT_SITE 308
FT /evidence="ECO:0000255"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 432 AA; 47895 MW; 870772E83104C1A2 CRC64;
MFRPNSLLIP SNLSTTKSQR NTMLNSSYLS FALIFFCCIL FSALASSLPV SDPELVVEEV
HRKINESISR RKLGFFSCGS GNPIDDCWRC DKDWEKNRKR LADCGIGFGK NAIGGRDGEI
YVVTDPGNDD PVNPRPGTLR YAVIQDEPLW IIFKRDMTIQ LKEELIMNSF KTLDGRGASV
HISGGPCITI QYVTNIIIHG LHIHDCKQGG NTYVRDSPEH YGYRTVSDGD GVSIFGGSHV
WVDHCSLSNC NDGLIDAIRG STAITISNNY LTHHNKVMLL GHSDTYEQDK NMQVTIAFNH
FGEGLVQRMP RCRHGYFHVV NNDYTHWEMY AIGGSANPTI NSQGNRFLAP DDSSSKEVTK
HEDAPEDEWR NWNWRSEGDL LLNGAFFTYS GAGPAKSSSY SKASSLAARP SSHVGEITIA
SGALSCKRGS HC
