BGL41_ARATH
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 03-AUG-2022, entry version 109.
DE RecName: Full=Putative beta-glucosidase 41;
DE Short=AtBGLU41;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU41; OrderedLocusNames=At5g54570; ORFNames=MRB17.7;
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 -!- 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.AT5G54570.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9FIU7; -.
DR PRIDE; Q9FIU7; -.
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; locus:2172134; AT5G54570.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9FIU7; -.
DR OrthoDB; 408001at2759; -.
DR BioCyc; ARA:AT5G54570-MON; -.
DR PRO; PR:Q9FIU7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIU7; baseline and differential.
DR Genevisible; Q9FIU7; AT.
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 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"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 470..471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 216..224
FT /evidence="ECO:0000250"
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
