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BXL4_ARATH
ID   BXL4_ARATH              Reviewed;         784 AA.
AC   Q9FLG1; Q56WR7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Beta-D-xylosidase 4;
DE            Short=AtBXL4;
DE            EC=3.2.1.37;
DE   Flags: Precursor;
GN   Name=BXL4; OrderedLocusNames=At5g64570; ORFNames=MUB3.9;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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] OF 262-784.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=12609041; DOI=10.1046/j.1365-313x.2003.01654.x;
RA   Goujon T., Minic Z., El Amrani A., Lerouxel O., Aletti E., Lapierre C.,
RA   Joseleau J.-P., Jouanin L.;
RT   "AtBXL1, a novel higher plant (Arabidopsis thaliana) putative beta-
RT   xylosidase gene, is involved in secondary cell wall metabolism and plant
RT   development.";
RL   Plant J. 33:677-690(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15181203; DOI=10.1104/pp.104.041269;
RA   Minic Z., Rihouey C., Do C.T., Lerouge P., Jouanin L.;
RT   "Purification and characterization of enzymes exhibiting beta-D-xylosidase
RT   activities in stem tissues of Arabidopsis.";
RL   Plant Physiol. 135:867-878(2004).
CC   -!- FUNCTION: Beta-D-xylosidase showing an optimal efficiency with the
CC       natural substrate xylobiose. {ECO:0000269|PubMed:15181203}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC         Evidence={ECO:0000269|PubMed:15181203};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.7 mM for p-nitrophenyl-beta-D-xylopyranoside
CC         {ECO:0000269|PubMed:15181203};
CC       pH dependence:
CC         Optimum pH is 4.7. {ECO:0000269|PubMed:15181203};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:15181203};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers, siliques and the apical part
CC       of the stems. {ECO:0000269|PubMed:12609041,
CC       ECO:0000269|PubMed:15181203}.
CC   -!- MISCELLANEOUS: Might be processed at the C-terminus.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; AB010076; BAB11424.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97922.1; -; Genomic_DNA.
DR   EMBL; AK221967; BAD94481.1; -; mRNA.
DR   RefSeq; NP_201262.1; NM_125853.3.
DR   AlphaFoldDB; Q9FLG1; -.
DR   SMR; Q9FLG1; -.
DR   STRING; 3702.AT5G64570.1; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   PaxDb; Q9FLG1; -.
DR   PRIDE; Q9FLG1; -.
DR   EnsemblPlants; AT5G64570.1; AT5G64570.1; AT5G64570.
DR   GeneID; 836578; -.
DR   Gramene; AT5G64570.1; AT5G64570.1; AT5G64570.
DR   KEGG; ath:AT5G64570; -.
DR   Araport; AT5G64570; -.
DR   TAIR; locus:2174809; AT5G64570.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   HOGENOM; CLU_004542_5_3_1; -.
DR   InParanoid; Q9FLG1; -.
DR   OMA; QCARDSN; -.
DR   OrthoDB; 321444at2759; -.
DR   PhylomeDB; Q9FLG1; -.
DR   BioCyc; ARA:AT5G64570-MON; -.
DR   BRENDA; 3.2.1.37; 399.
DR   SABIO-RK; Q9FLG1; -.
DR   PRO; PR:Q9FLG1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLG1; baseline and differential.
DR   Genevisible; Q9FLG1; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0016020; C:membrane; HDA:TAIR.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IBA:GO_Central.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:TAIR.
DR   GO; GO:0031222; P:arabinan catabolic process; IBA:GO_Central.
DR   GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:TAIR.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42721; PTHR42721; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..784
FT                   /note="Beta-D-xylosidase 4"
FT                   /id="PRO_0000384059"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        263
FT                   /note="C -> Y (in Ref. 3; BAD94481)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="H -> R (in Ref. 3; BAD94481)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   784 AA;  84308 MW;  52D404092378771A CRC64;
     MGSSSPLTRR NRAPPSSVSS VYLIFLCFFL YFLNFSNAQS SPVFACDVAA NPSLAAYGFC
     NTVLKIEYRV ADLVARLTLQ EKIGFLVSKA NGVTRLGIPT YEWWSEALHG VSYIGPGTHF
     SSQVPGATSF PQVILTAASF NVSLFQAIGK VVSTEARAMY NVGLAGLTYW SPNVNIFRDP
     RWGRGQETPG EDPLLASKYA SGYVKGLQET DGGDSNRLKV AACCKHYTAY DVDNWKGVER
     YSFNAVVTQQ DMDDTYQPPF KSCVVDGNVA SVMCSYNQVN GKPTCADPDL LSGVIRGEWK
     LNGYIVSDCD SVDVLYKNQH YTKTPAEAAA ISILAGLDLN CGSFLGQHTE EAVKSGLVNE
     AAIDKAISNN FLTLMRLGFF DGNPKNQIYG GLGPTDVCTS ANQELAADAA RQGIVLLKNT
     GCLPLSPKSI KTLAVIGPNA NVTKTMIGNY EGTPCKYTTP LQGLAGTVST TYLPGCSNVA
     CAVADVAGAT KLAATADVSV LVIGADQSIE AESRDRVDLH LPGQQQELVI QVAKAAKGPV
     LLVIMSGGGF DITFAKNDPK IAGILWVGYP GEAGGIAIAD IIFGRYNPSG KLPMTWYPQS
     YVEKVPMTIM NMRPDKASGY PGRTYRFYTG ETVYAFGDGL SYTKFSHTLV KAPSLVSLGL
     EENHVCRSSE CQSLDAIGPH CENAVSGGGS AFEVHIKVRN GGDREGIHTV FLFTTPPAIH
     GSPRKHLVGF EKIRLGKREE AVVRFKVEIC KDLSVVDEIG KRKIGLGKHL LHVGDLKHSL
     SIRI
 
 
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