ID   BGL02_ARATH             Reviewed;         299 AA.
AC   Q9FMD8;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=Putative beta-glucosidase 2 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU2 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE   Flags: Precursor;
GN   Name=BGLU2 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At5g16580 {ECO:0000312|Araport:AT5G16580};
GN   ORFNames=MTG13.2 {ECO:0000312|EMBL:BAB10185.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB008270; BAB10185.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92313.1; -; Genomic_DNA.
DR   RefSeq; NP_197161.2; NM_121664.3.
DR   AlphaFoldDB; Q9FMD8; -.
DR   SMR; Q9FMD8; -.
DR   STRING; 3702.Q9FMD8; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9FMD8; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT5G16580-1; -.
DR   EnsemblPlants; AT5G16580.1; AT5G16580.1; AT5G16580.
DR   GeneID; 831520; -.
DR   Gramene; AT5G16580.1; AT5G16580.1; AT5G16580.
DR   KEGG; ath:AT5G16580; -.
DR   Araport; AT5G16580; -.
DR   TAIR; AT5G16580; BGLU2.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_4_0_1; -.
DR   InParanoid; Q9FMD8; -.
DR   OMA; FPWAMES; -.
DR   OrthoDB; 3373839at2759; -.
DR   PhylomeDB; Q9FMD8; -.
DR   BioCyc; ARA:AT5G16580-MONOMER; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMD8; 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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF150; BETA-GLUCOSIDASE 1-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   Genevisible; Q9FMD8; AT.
PE   5: Uncertain;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..299
FT                   /note="Putative beta-glucosidase 2"
FT                   /id="PRO_0000389564"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        255
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         49..50
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         189
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         255
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        69..72
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   299 AA;  33646 MW;  4877F49F6248C5C5 CRC64;
     MLHCITTIFL SISRMTMEDG PIAESYFTAY ADVCFREFGN HVKFWTTINE ANVFTIGGYN
     DGTSPPGRCS NCSSGNSSTE TYIVGHNLLL AHASVSRLYQ QKYKDKQGGS VGFSLYAFEF
     IPQTSSSKDD EIAIQRAKDF FYGWILGPLT FGDYPDEMKR AVGSRLPIFS KEESEQVKGS
     SDFIGIMHYF PALVENIKLK PSLSRNTDFY SDMGVSLTYL GNFSGFGYDV FPWAMESVLE
     YIKQTYGNPP VYILENGTPM KPDLELQQKD TRRIEYLQAY IGAVLKAVRN GSDTRGYFV
//