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PLY7_ARATH
ID   PLY7_ARATH              Reviewed;         475 AA.
AC   Q9SRH4; Q8LGC8;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable pectate lyase 7;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g01270; ORFNames=T22N4.10, T4P13.4;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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.
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; AC008261; AAF26147.1; -; Genomic_DNA.
DR   EMBL; AC010676; AAF03499.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73631.1; -; Genomic_DNA.
DR   EMBL; AY084341; AAM60924.1; -; mRNA.
DR   RefSeq; NP_186776.1; NM_110993.4.
DR   AlphaFoldDB; Q9SRH4; -.
DR   SMR; Q9SRH4; -.
DR   STRING; 3702.AT3G01270.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; Q9SRH4; -.
DR   PRIDE; Q9SRH4; -.
DR   ProteomicsDB; 235048; -.
DR   EnsemblPlants; AT3G01270.1; AT3G01270.1; AT3G01270.
DR   GeneID; 821142; -.
DR   Gramene; AT3G01270.1; AT3G01270.1; AT3G01270.
DR   KEGG; ath:AT3G01270; -.
DR   Araport; AT3G01270; -.
DR   TAIR; locus:2100247; AT3G01270.
DR   eggNOG; ENOG502QQE2; Eukaryota.
DR   HOGENOM; CLU_026608_0_1_1; -.
DR   InParanoid; Q9SRH4; -.
DR   OMA; CQELMIN; -.
DR   OrthoDB; 924221at2759; -.
DR   PhylomeDB; Q9SRH4; -.
DR   BioCyc; ARA:AT3G01270-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:Q9SRH4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SRH4; baseline and differential.
DR   Genevisible; Q9SRH4; 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; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..475
FT                   /note="Probable pectate lyase 7"
FT                   /id="PRO_0000024871"
FT   REGION          91..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000255"
FT   BINDING         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        28
FT                   /note="D -> E (in Ref. 3; AAM60924)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="V -> I (in Ref. 3; AAM60924)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   475 AA;  53855 MW;  DE1550EA09B8161D CRC64;
     METARLFKLV CVICIASLIP TIRANVADET DEYWVNKANE ARKHTLMAYH PDPYEIVDHF
     HERHYDNSTD VEGTEEEKAV ASEEEDVIEM ISSPTNSTRR SLTGRGKGKG KGKWSKLTGP
     CTASNPIDKC WRCQPDWARR RKKLVHCVRG FGYRTTGGKR GRIYVVTSPR DDDMVNPRPG
     TLRHAVIQKE PLWIVFKHDM SIRLSQELMI TSDKTIDARG ANVHIAYGAG ITMQYVHNII
     IHGLHVHHIV KSSGGLIRDS INHFGHRGEA DGDGISIFGA TNIWLDHISM SKCQDGLIDA
     IMGSTAITIS NSHFTHHNDV MLLGAQNNNM DDKKMQVTVA YNHFGKGLVQ RMPRVRWGFV
     HVVNNDYTHW ELYAIGGSQG PTILSHGNRF IAPPHKQHYR EVTKRDYASE SEWKNWNWRS
     EKDVFMNNAY FRQSGNPHFK CSHSRQQMIK PKNGMAVSKL TKYAGALDCR VGKAC
 
 
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