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PLY6_ARATH
ID   PLY6_ARATH              Reviewed;         455 AA.
AC   O64510;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Probable pectate lyase 6;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g02720; ORFNames=T20F6.14;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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).
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; AC002521; AAC05350.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05615.1; -; Genomic_DNA.
DR   EMBL; BT005757; AAO64162.1; -; mRNA.
DR   PIR; T00856; T00856.
DR   RefSeq; NP_178375.1; NM_126327.4.
DR   AlphaFoldDB; O64510; -.
DR   SMR; O64510; -.
DR   STRING; 3702.AT2G02720.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; O64510; -.
DR   PRIDE; O64510; -.
DR   ProteomicsDB; 234929; -.
DR   EnsemblPlants; AT2G02720.1; AT2G02720.1; AT2G02720.
DR   GeneID; 814801; -.
DR   Gramene; AT2G02720.1; AT2G02720.1; AT2G02720.
DR   KEGG; ath:AT2G02720; -.
DR   Araport; AT2G02720; -.
DR   TAIR; locus:2058842; AT2G02720.
DR   eggNOG; ENOG502QQE2; Eukaryota.
DR   HOGENOM; CLU_026608_2_1_1; -.
DR   InParanoid; O64510; -.
DR   OMA; CKEYVKC; -.
DR   OrthoDB; 924221at2759; -.
DR   PhylomeDB; O64510; -.
DR   BioCyc; ARA:AT2G02720-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:O64510; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64510; baseline and differential.
DR   Genevisible; O64510; 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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..455
FT                   /note="Probable pectate lyase 6"
FT                   /id="PRO_0000024870"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000255"
FT   BINDING         247
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
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   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   455 AA;  51258 MW;  7C6A35A767A30CA4 CRC64;
     MVNLGSYVFV FVALSLTVVV PSVQAHIAEY DEYWTQRQTN ALRETLESYD PNPENVTDHF
     NYHAALAMET TGIVNETRRD LRQVGRGKKT TRRGGRFESL NAIDKCWRGD KNWDKNRKKL
     ADCVLGFGRK TTGGKNGPIY VVTDPSDNDL LKPKPGTIRH AVTRDRPLWI IFARSMIIKL
     QQELIITNDK TIDGRGAKIY ITGGAGLTLQ FVRNVIIHNI HIKQIKRGAG GLIIDSEQHF
     GLRTVSDGDG INIFGATNVW IDHVSMTDCS DGMIDAIMGS TAITISNSHF TDHDEVMLFG
     GTNKDVIDKK MQITVAFNHF GKRLKQRMPR VRFGLVHVVN NDYTHWEMYA IGGNMNPTII
     SQGNRFIAPP IEDSKQVTKR EYTPYPEWKS WNWQSEKDYF LNGAYFVQSG KANAWSATPK
     NPIPRKFAIR PQPGTKVRRL TKDAGTLGCK PGKSC
 
 
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