BGL08_ARATH
ID BGL08_ARATH Reviewed; 497 AA.
AC Q67XN2; Q67XI6; Q9LZJ0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Beta-glucosidase 8;
DE Short=AtBGLU8;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU8; OrderedLocusNames=At3g62750; ORFNames=F26K9.180;
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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD44596.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB83125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162651; CAB83125.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80387.1; -; Genomic_DNA.
DR EMBL; AK175256; BAD43019.1; -; mRNA.
DR EMBL; AK176786; BAD44549.1; -; mRNA.
DR EMBL; AK176833; BAD44596.1; ALT_FRAME; mRNA.
DR PIR; T48064; T48064.
DR RefSeq; NP_191834.3; NM_116140.4.
DR AlphaFoldDB; Q67XN2; -.
DR SMR; Q67XN2; -.
DR STRING; 3702.AT3G62750.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q67XN2; -.
DR PRIDE; Q67XN2; -.
DR ProteomicsDB; 240332; -.
DR EnsemblPlants; AT3G62750.1; AT3G62750.1; AT3G62750.
DR GeneID; 825450; -.
DR Gramene; AT3G62750.1; AT3G62750.1; AT3G62750.
DR KEGG; ath:AT3G62750; -.
DR Araport; AT3G62750; -.
DR TAIR; locus:2081680; AT3G62750.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q67XN2; -.
DR PhylomeDB; Q67XN2; -.
DR PRO; PR:Q67XN2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q67XN2; baseline and differential.
DR Genevisible; Q67XN2; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
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 2: Evidence at transcript level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..497
FT /note="Beta-glucosidase 8"
FT /id="PRO_0000389570"
FT ACT_SITE 185
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 437..438
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 56178 MW; 6FC878F48043BEAF CRC64;
MKHFNLLSII LVIVLATSYI DAFTRNDFPE DFLFGAGTSA YQWEGAANED GRTPSVWDTT
SHCYNGSNGD IACDGYHKYK EDVKLMAEMG LESFRFSISW SRLIPNGRGR INPKGLLFYK
NLIKELRSHG IEPHVTLYHY DLPQSLEDEY GGWINHKIIE DFTAFADVCF REFGEDVKLW
TTINEATIFA FAFYGKDVRY GNCTTGNYCM ETYIAGHNML LAHASASNLY KLKYKSKQRG
SIGLSIFALG LTPYTNSKDD EIATQRAKAF LYGWMLKPLV FGDYPDEMKR TLGSRLPVFS
EEESEQVKGS SDFVGIIHYT TVYVTNQPAP YIFPSSTNKD FFTDMGAYII STGNSSSFVF
DAVPWGLEGV LQHIKHRYNN PPIYILENGS PMKHDSMLQD TPRVEYIQAY IGAVLNAIKS
GSDTRGYFVW SLIDLFEVQV GYKSSFGMYY VNFSDPGRKR SPKLSASWYT GFLNGTIDVA
SQDMTQLQRN FSGSSSL
