ID   BGL41_ARATH             Reviewed;         535 AA.
AC   Q9FIU7;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Putative beta-glucosidase 41 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU41 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE   Flags: Precursor;
GN   Name=BGLU41 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At5g54570 {ECO:0000312|Araport:AT5G54570};
GN   ORFNames=MRB17.7 {ECO:0000312|EMBL:BAB09336.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(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   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=BAB09336.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB016879; BAB09336.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96511.1; -; Genomic_DNA.
DR   RefSeq; NP_200268.3; NM_124837.3.
DR   AlphaFoldDB; Q9FIU7; -.
DR   SMR; Q9FIU7; -.
DR   STRING; 3702.Q9FIU7; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9FIU7; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT5G54570-1; -.
DR   ProteomicsDB; 240622; -.
DR   EnsemblPlants; AT5G54570.1; AT5G54570.1; AT5G54570.
DR   GeneID; 835545; -.
DR   Gramene; AT5G54570.1; AT5G54570.1; AT5G54570.
DR   KEGG; ath:AT5G54570; -.
DR   Araport; AT5G54570; -.
DR   TAIR; AT5G54570; BGLU41.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9FIU7; -.
DR   OrthoDB; 3373839at2759; -.
DR   BioCyc; ARA:AT5G54570-MONOMER; -.
DR   PRO; PR:Q9FIU7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIU7; baseline and differential.
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:SF345; BETA-GLUCOSIDASE 41-RELATED; 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.
DR   Genevisible; Q9FIU7; AT.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..535
FT                   /note="Putative beta-glucosidase 41"
FT                   /id="PRO_0000390314"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        413
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         49
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         413
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         463
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         470..471
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         479
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        489
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   535 AA;  61463 MW;  A8676E96B6F119F2 CRC64;
     MESLMRLVLV LFPFFVVFFV PLDHVSSESI SRANFPDGFV FGTASSAYQF EGAVKEGNKG
     ESIWDTFTKE KPGKILDFSN ADTTVDQYHR FHNDIDLMKD LRMDAYRFSI SWSRIFPNGT
     GEVNPDGVKY YNSLIDALLA KGIKPYVTLY HWDLPQALED RYEGWLSREV VDDFEHYAFT
     CFKAFGDRVK YWITFNEPHG VSIQGYDTGI QAPGRCSLLG HWFCKKGKSS VEPYIVAHNI
     LLSHAAAYHT YQRNFKEKQR GQIGISLDAK WYEPMSDCDE DKDAARRAMD FGLGWFMDPL
     INGDYPASMK SLVEERLPKI TPEMYKTIKG AFDYVGINHY TTLYARNDRT RIRKLILQDA
     SSDSAVITSS FRGGVAIGER AGSSWLHIVP WGIRKLAVYV KDIYGNPPVF ITENGMDEKN
     SPFIDMEKAL KDDKRIGFHR DYLSNLSAAI RNDECDVRGY FVWSLLDNWE WNSGYTVRFG
     IYYVDYKNNL TRIPKASARW FQTILSGSSS TSDSSKLILL EEATEQQQEY KFQEK
//