PLY3_ARATH
ID PLY3_ARATH Reviewed; 459 AA.
AC Q9M9S2; O23665;
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 3;
DE EC=4.2.2.2;
DE AltName: Full=Pectate lyase A2;
DE Flags: Precursor;
GN Name=AT59; OrderedLocusNames=At1g14420; ORFNames=F14L17.19;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9278171; DOI=10.1023/a:1005856531693;
RA Kulikauskas R., McCormick S.;
RT "Identification of the tobacco and Arabidopsis homologues of the pollen-
RT expressed LAT59 gene of tomato.";
RL Plant Mol. Biol. 34:809-814(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 -!- TISSUE SPECIFICITY: Expressed in pollen, but not in leaves.
CC {ECO:0000269|PubMed:9278171}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
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DR EMBL; U83619; AAB69759.1; -; Genomic_DNA.
DR EMBL; AC012188; AAF43942.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29161.1; -; Genomic_DNA.
DR EMBL; BT010451; AAQ62871.1; -; mRNA.
DR PIR; G86278; G86278.
DR RefSeq; NP_172894.1; NM_101309.5.
DR AlphaFoldDB; Q9M9S2; -.
DR SMR; Q9M9S2; -.
DR STRING; 3702.AT1G14420.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q9M9S2; -.
DR PRIDE; Q9M9S2; -.
DR ProteomicsDB; 234974; -.
DR EnsemblPlants; AT1G14420.1; AT1G14420.1; AT1G14420.
DR GeneID; 838004; -.
DR Gramene; AT1G14420.1; AT1G14420.1; AT1G14420.
DR KEGG; ath:AT1G14420; -.
DR Araport; AT1G14420; -.
DR TAIR; locus:2012562; AT1G14420.
DR eggNOG; ENOG502QQE2; Eukaryota.
DR HOGENOM; CLU_026608_2_1_1; -.
DR InParanoid; Q9M9S2; -.
DR OMA; GYLFVFC; -.
DR OrthoDB; 924221at2759; -.
DR PhylomeDB; Q9M9S2; -.
DR BioCyc; ARA:AT1G14420-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q9M9S2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9S2; baseline and differential.
DR Genevisible; Q9M9S2; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; ISS:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009664; P:plant-type cell wall organization; TAS:TAIR.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..459
FT /note="Probable pectate lyase 3"
FT /id="PRO_0000024867"
FT ACT_SITE 331
FT /evidence="ECO:0000255"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 258
FT /note="F -> I (in Ref. 1; AAB69759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 51455 MW; 634FBB54FEDCBA17 CRC64;
MAAAFLNLGG YVFVFFSSFL AIVAPQVRGN VAVFDSYWTQ RQSDALKQTI GSYDPHPLNV
TNHFNYHVNI AVDASESRND TRRELTQVRS GRKTHKSSGK CLAYNPIDNC WRCDRNWANN
RKKLADCVLG FGRRTTGGKD GPIYVVKDAS DNDLINPKPG TLRHAVTRDG PLWIIFARSM
IIKLQQELMI TSDKTIDGRG ARVYIMEGAG LTLQFVNNVI IHNIYVKHIV PGNGGLIRDS
EAHIGLRTKS DGDGISLFGA TNIWIDHVSM TRCADGMIDA IDGSTAVTIS NSHFTDHQEV
MLFGARDEHV IDKKMQITVA FNHFGKRLEQ RMPRCRYGTI HVVNNDYTHW EMYAIGGNMN
PTIISQGNRF IAPPNEEAKQ ITKREYTPYG EWKSWNWQSE GDYFLNGAYF VQSGKANAWS
SKPKTPLPNK FTIRPKPGTM VRKLTMDAGV LGCKLGEAC
