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PLY9_ARATH
ID   PLY9_ARATH              Reviewed;         452 AA.
AC   Q9LRM5;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable pectate lyase 9;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g24230; ORFNames=MUJ8.14;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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}.
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DR   EMBL; AB028621; BAB01365.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76877.1; -; Genomic_DNA.
DR   EMBL; BX823056; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_189065.2; NM_113328.3.
DR   AlphaFoldDB; Q9LRM5; -.
DR   SMR; Q9LRM5; -.
DR   STRING; 3702.AT3G24230.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; Q9LRM5; -.
DR   PRIDE; Q9LRM5; -.
DR   EnsemblPlants; AT3G24230.1; AT3G24230.1; AT3G24230.
DR   GeneID; 822010; -.
DR   Gramene; AT3G24230.1; AT3G24230.1; AT3G24230.
DR   KEGG; ath:AT3G24230; -.
DR   Araport; AT3G24230; -.
DR   TAIR; locus:2093761; AT3G24230.
DR   eggNOG; ENOG502QQ5F; Eukaryota.
DR   HOGENOM; CLU_026608_0_1_1; -.
DR   InParanoid; Q9LRM5; -.
DR   OMA; HMSEQNI; -.
DR   OrthoDB; 582220at2759; -.
DR   PhylomeDB; Q9LRM5; -.
DR   BioCyc; ARA:AT3G24230-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:Q9LRM5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LRM5; baseline and differential.
DR   Genevisible; Q9LRM5; 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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..452
FT                   /note="Probable pectate lyase 9"
FT                   /id="PRO_0000024873"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000255"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        224
FT                   /note="H -> N (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="D -> H (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="G -> A (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="Y -> H (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="Y -> H (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="F -> S (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="D -> H (in Ref. 3; BX823056)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   452 AA;  49985 MW;  F31AD9097F923249 CRC64;
     MATSSLKLTS ACFVLLFIFV GCVLTATNLR NNEISRSRKL KTEDSKSFNS SPMTTRLDGV
     VELNEHAVTD PDKVAHEVSN LIHMSEQNIT ARRKLGFFSC GNGNLIDDCW RCDRNWNKNR
     KHLADCGMGF GSKAFGGRNG SYYVVTDHSD DDVVNPKPGT LRHAVIQVEP LWIIFKRDMV
     IKLKQELIMN SFKTIDARGA NVHIANGACI TIQNITNVIV HGLHIHDCKR TGNVTVRSSP
     SQAGFRGTAD GDAINIFGSS HIWIDHNSLS NCTDGLVDVV NGSTAITISN NHFTHHDEVM
     LLGHNDSYTR DKMMQVTVAY NHFGEGLIQR MPRCRHGYFH VVNNDYTHWK MYAIGGSANP
     TINSQGNRFA APKNHSAKEV TKRLDTKGNE WMEWNWRSEK DLLVNGAFFT PSGEGASGDS
     QTLSLPAKPA SMVDAITASA GALSCRRGKP CY
 
 
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