ID BGL28_ARATH Reviewed; 582 AA.
AC Q4V3B3; O64880;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Beta-glucosidase 28 {ECO:0000303|PubMed:15604686};
DE Short=AtBGLU28 {ECO:0000303|PubMed:15604686};
DE EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE Flags: Precursor;
GN Name=BGLU28 {ECO:0000303|PubMed:15604686};
GN OrderedLocusNames=At2g44460 {ECO:0000312|Araport:AT2G44460};
GN ORFNames=F4I1.27 {ECO:0000312|EMBL:AAC16092.1};
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) 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 Evidence={ECO:0000250|UniProtKB:O64879};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC16092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004521; AAC16092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10422.1; -; Genomic_DNA.
DR EMBL; BT023443; AAY56434.1; -; mRNA.
DR PIR; T02401; T02401.
DR RefSeq; NP_850416.1; NM_180085.4.
DR AlphaFoldDB; Q4V3B3; -.
DR SMR; Q4V3B3; -.
DR STRING; 3702.Q4V3B3; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GlyCosmos; Q4V3B3; 6 sites, No reported glycans.
DR PaxDb; 3702-AT2G44460-1; -.
DR ProteomicsDB; 241214; -.
DR EnsemblPlants; AT2G44460.1; AT2G44460.1; AT2G44460.
DR GeneID; 819053; -.
DR Gramene; AT2G44460.1; AT2G44460.1; AT2G44460.
DR KEGG; ath:AT2G44460; -.
DR Araport; AT2G44460; -.
DR TAIR; AT2G44460; BGLU28.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q4V3B3; -.
DR OMA; VRTIIYH; -.
DR OrthoDB; 640576at2759; -.
DR PhylomeDB; Q4V3B3; -.
DR BioCyc; ARA:AT2G44460-MONOMER; -.
DR PRO; PR:Q4V3B3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q4V3B3; baseline and differential.
DR Genevisible; Q4V3B3; AT.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF253; BETA-GLUCOSIDASE 28; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..582
FT /note="Beta-glucosidase 28"
FT /id="PRO_0000389590"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 48
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 151
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 196..197
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 340
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 412
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT BINDING 462
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 469..470
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 478
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 216..224
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ SEQUENCE 582 AA; 67299 MW; 6F551146E571F180 CRC64;
MKMHFFILLV ITSWLSEKIT SLPPDSRVFD RHGFPDNFVF GTAASAFQYE GATSEGGKSP
SIWDYFSHTF PERTRMQNAD VAVDFYHRYK DDIKLMKELN MDAFRFSISW ARLIPSGKVK
DGVNKEGVEF YKALIDELVA NGIEPSMTLY HWDHPQSLED EYGGFLSPQI VEDFRDFSRV
CFEEFGDKVK MWTTINEPYV ITVAGYDTGN KAVGRCSKWV NSKCQGGDSG TEPYIASHHL
LLAHAAAVQE FRKCNKTQDG QIGIVLSPLW FEPYDSASPA DNEAVKRALA TELDWHLDPV
IHGDYPEMMK KLAGNRLPSF TPEQSKMLKN SSDFIGINYY TARYVAHIPQ ADPARPRFVT
DHQLQWRVTN HSNHQFGPGE DRGILQSHPE GLRKVLNYIK DKYNNPIVYI KENGINDYDD
GTKSREEILN DTFRISYHED HLQQLQKAII EDGCDVRGYY VWSLLDNFEW EHGYSTRFGV
YYVDYDNDLT RIPKDSVNWF KQFLDVKNKE IWDVSHKERY NKTFDDVESF EASVGSILYL
MTNNISRREE EERDQCAFGN LNDQSGLLLE SYNSFGFLEN VW
//
