PLY1_ARATH
ID PLY1_ARATH Reviewed; 431 AA.
AC Q940Q1; O23017; O23666;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable pectate lyase 1;
DE EC=4.2.2.2;
DE AltName: Full=Pectate lyase A1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g04680; ORFNames=T1G11.7, T1G11_6;
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=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 [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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-275, 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).
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 flowers, but not in leaves.
CC {ECO:0000269|PubMed:9278171}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL06861.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL47400.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC002376; AAB80622.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27732.1; -; Genomic_DNA.
DR EMBL; AY065034; AAL57671.1; -; mRNA.
DR EMBL; AY054200; AAL06861.1; ALT_FRAME; mRNA.
DR EMBL; AY066033; AAL47400.1; ALT_FRAME; mRNA.
DR EMBL; AY087724; AAM65261.1; -; mRNA.
DR EMBL; U83620; AAB69760.1; -; Genomic_DNA.
DR PIR; F86179; F86179.
DR RefSeq; NP_563715.1; NM_100348.4.
DR AlphaFoldDB; Q940Q1; -.
DR SMR; Q940Q1; -.
DR BioGRID; 24687; 1.
DR STRING; 3702.AT1G04680.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q940Q1; -.
DR PRIDE; Q940Q1; -.
DR ProteomicsDB; 226148; -.
DR EnsemblPlants; AT1G04680.1; AT1G04680.1; AT1G04680.
DR GeneID; 839452; -.
DR Gramene; AT1G04680.1; AT1G04680.1; AT1G04680.
DR KEGG; ath:AT1G04680; -.
DR Araport; AT1G04680; -.
DR TAIR; locus:2197808; AT1G04680.
DR eggNOG; ENOG502QQ5F; Eukaryota.
DR HOGENOM; CLU_026608_0_1_1; -.
DR InParanoid; Q940Q1; -.
DR OMA; YMRDKAM; -.
DR OrthoDB; 582220at2759; -.
DR PhylomeDB; Q940Q1; -.
DR BioCyc; ARA:AT1G04680-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q940Q1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940Q1; baseline and differential.
DR Genevisible; Q940Q1; 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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..431
FT /note="Probable pectate lyase 1"
FT /id="PRO_0000024865"
FT ACT_SITE 307
FT /evidence="ECO:0000255"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 151
FT /note="V -> I (in Ref. 5; AAB69760)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Missing (in Ref. 5; AAB69760)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..257
FT /note="DAV -> ERS (in Ref. 5; AAB69760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47771 MW; 241D3FD68D55C832 CRC64;
MAVLPTWLLA MMCLLFFVGA MENTTHDNIS SLPRSDETEW NQHAVTNPDE VADEVLALTE
MSVRNHTERR KLGYFTCGTG NPIDDCWRCD PNWHKNRKRL ADCGIGFGRN AIGGRDGRFY
VVTDPRDDNP VNPRPGTLRH AVIQDRPLWI VFKRDMVIQL KQELIVNSFK TIDGRGANVH
IANGGCITIQ FVTNVIVHGL HIHDCKPTGN AMVRSSETHF GWRTMADGDA ISIFGSSHVW
IDHNSLSHCA DGLVDAVMGS TAITISNNHL THHNEVMLLG HSDSYMRDKA MQVTIAYNHF
GVGLIQRMPR CRHGYFHVVN NDYTHWEMYA IGGSANPTIN SQGNRYAAPK NPFAKEVTKR
VDTPASHWKG WNWRSEGDLL QNGAYFTSSG AAASGSYARA SSLSAKSSSL VGHITSDAGA
LPCRRGRQCS S
