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BGL01_ARATH
ID   BGL01_ARATH             Reviewed;         517 AA.
AC   Q3ECW8; F4HRB1; F4HRB2;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Beta-glucosidase 1;
DE            Short=AtBGLU1;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU1; OrderedLocusNames=At1g45191; ORFNames=T2P3;
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).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA   Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA   Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT   "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT   family 1.";
RL   Plant Mol. Biol. 55:343-367(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q3ECW8-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE32093.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AEE32094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC084820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE32093.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32094.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; ANM60926.1; -; Genomic_DNA.
DR   RefSeq; NP_001323174.1; NM_001333250.1. [Q3ECW8-1]
DR   RefSeq; NP_849771.2; NM_179440.2.
DR   RefSeq; NP_973974.2; NM_202245.2.
DR   AlphaFoldDB; Q3ECW8; -.
DR   SMR; Q3ECW8; -.
DR   STRING; 3702.AT1G45191.1; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; Q3ECW8; -.
DR   PRIDE; Q3ECW8; -.
DR   ProteomicsDB; 240463; -. [Q3ECW8-1]
DR   EnsemblPlants; AT1G45191.6; AT1G45191.6; AT1G45191. [Q3ECW8-1]
DR   GeneID; 841088; -.
DR   Gramene; AT1G45191.6; AT1G45191.6; AT1G45191. [Q3ECW8-1]
DR   KEGG; ath:AT1G45191; -.
DR   Araport; AT1G45191; -.
DR   TAIR; locus:1005716680; AT1G45191.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q3ECW8; -.
DR   OrthoDB; 408001at2759; -.
DR   BioCyc; ARA:AT1G45191-MON; -.
DR   PRO; PR:Q3ECW8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q3ECW8; baseline and differential.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..517
FT                   /note="Beta-glucosidase 1"
FT                   /id="PRO_0000389563"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         458..459
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        210..217
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  58585 MW;  726DA4B0420B2EAC CRC64;
     MEDVLTLITM IVLLLLAFHG FGKCSSDLYS RSDFPEGFVF GAGISAYQWE GAVDEDGRKP
     SVWDTFLHCR KMDNGDIACD GYHKYKEDVQ LMAETGLHTF RFSISWSRLI SNGRGSINPK
     GLQFYKNFIQ ELVKHGIEPH VTLHHYDFPQ YLEDDYGGWT NRKIIKDFTA YADVCFREFG
     NHVKFWTTIN EANIFTIGGY NDGNSPPGRC SFPGRNCTLG NSSTETYIVG HNLLLAHASV
     SRLYKQKYKD IQGGSVGFSL FAMNFTPSTN SKDDEIATKR ANDFYLGWML EPLIYGDYPD
     VMKRTIGSRL PVFSKEESEQ VKGSSDFIGV IHYLTALVTN IDINPSLSGI PDFNSDMGES
     INILSMRVRI SRLPNSDEKC LIFFITLSIL EYIKQSYGNP PVYILENGKT MNQDLELQQK
     DTPRIEYLDA YIGAVLKAVR NGSDTRGYFV WSFMDLYELL NGYKSSFGLY SVNFSDPHRK
     RSPKLSAHWY SGFLKGKPTF LGSQGITQLH SNFSSSR
 
 
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