PLY2_ARATH
ID PLY2_ARATH Reviewed; 384 AA.
AC O65388; F4IAK2;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative pectate lyase 2;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN OrderedLocusNames=At1g11920; ORFNames=F12F1.22;
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).
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=AAC17625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002131; AAC17625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28815.1; -; Genomic_DNA.
DR PIR; H86253; H86253.
DR RefSeq; NP_172656.1; NM_101064.2.
DR AlphaFoldDB; O65388; -.
DR SMR; O65388; -.
DR STRING; 3702.AT1G11920.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; O65388; -.
DR PRIDE; O65388; -.
DR ProteomicsDB; 234926; -.
DR EnsemblPlants; AT1G11920.1; AT1G11920.1; AT1G11920.
DR GeneID; 837742; -.
DR Gramene; AT1G11920.1; AT1G11920.1; AT1G11920.
DR KEGG; ath:AT1G11920; -.
DR Araport; AT1G11920; -.
DR TAIR; locus:2008925; AT1G11920.
DR eggNOG; ENOG502QSYA; Eukaryota.
DR HOGENOM; CLU_026608_0_1_1; -.
DR InParanoid; O65388; -.
DR OMA; HCYSGRI; -.
DR OrthoDB; 924221at2759; -.
DR BioCyc; ARA:AT1G11920-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:O65388; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65388; baseline and differential.
DR Genevisible; O65388; 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 3: Inferred from homology;
KW Calcium; Lyase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..384
FT /note="Putative pectate lyase 2"
FT /id="PRO_0000024866"
FT ACT_SITE 262
FT /evidence="ECO:0000255"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 42693 MW; 0BA653FC08194A21 CRC64;
MASLFLTIIS LLFAAFSSSV VEAAYSNGYT IPKLLPNPID SCWRRNPYWA SNRRALADCA
VGFGKSAVGG KYGSIYVVTN PSDDPENPRP GTLRYAVIQS KPLWITFARD MVIVLRNELI
MNSYKTIDGR GAKVEIAYGP CITIQHVSHV IIHGISIHDC KPGKSGRVRS SPTHVGSRKG
SDGDAIAIFD SSHIWIDHCF FSRCQDGLID VLHASTAVTI SNNYFTQHDK VMLLGHNDNN
VEDKIMRVTI AFNHFGPGLI ERMPRVRRGY AHVANNRYEK WQMYAIGGSA DPTIFSEGNY
FVASDDPSKK QVTKRIDSGY DWKRWKWRTS KDVFKNGAYF VPSGYGTVTP LYGRAERFPV
SHGSLVPLLT SSAGPLHCYS GRIC
