ID   BGL45_ARATH             Reviewed;         520 AA.
AC   O80689;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Beta-glucosidase 45 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU45 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:16814332};
DE   Flags: Precursor;
GN   Name=BGLU45 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At1g61810 {ECO:0000312|Araport:AT1G61810};
GN   ORFNames=F8K4.2 {ECO:0000312|EMBL:AAC28501.1}, T13M11.19;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   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).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16814332; DOI=10.1016/j.phytochem.2006.05.022;
RA   Escamilla-Trevino L.L., Chen W., Card M.L., Shih M.-C., Cheng C.-L.,
RA   Poulton J.E.;
RT   "Arabidopsis thaliana beta-glucosidases BGLU45 and BGLU46 hydrolyse
RT   monolignol glucosides.";
RL   Phytochemistry 67:1651-1660(2006).
CC   -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside and natural
CC       glucosides such as syringin, coniferin and p-coumaryl alcohol
CC       glucoside. May be involved in lignification by hydrolyzing monolignol
CC       glucosides. {ECO:0000269|PubMed:16814332}.
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:0000269|PubMed:16814332};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.4 mM for syringin (at pH 5.5) {ECO:0000269|PubMed:16814332};
CC         KM=7 mM for coniferin (at pH 5.5) {ECO:0000269|PubMed:16814332};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O80689-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in stems and siliques.
CC       {ECO:0000269|PubMed:16814332}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AC004392; AAC28501.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33890.1; -; Genomic_DNA.
DR   PIR; T02127; T02127.
DR   RefSeq; NP_176374.1; NM_104863.3. [O80689-1]
DR   AlphaFoldDB; O80689; -.
DR   SMR; O80689; -.
DR   STRING; 3702.O80689; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; O80689; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT1G61810-3; -.
DR   ProteomicsDB; 240373; -. [O80689-1]
DR   EnsemblPlants; AT1G61810.1; AT1G61810.1; AT1G61810. [O80689-1]
DR   GeneID; 842478; -.
DR   Gramene; AT1G61810.1; AT1G61810.1; AT1G61810. [O80689-1]
DR   KEGG; ath:AT1G61810; -.
DR   Araport; AT1G61810; -.
DR   TAIR; AT1G61810; BGLU45.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; O80689; -.
DR   OMA; TENGYAT; -.
DR   PhylomeDB; O80689; -.
DR   BioCyc; ARA:AT1G61810-MONOMER; -.
DR   SABIO-RK; O80689; -.
DR   PRO; PR:O80689; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O80689; baseline and differential.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0047782; F:coniferin beta-glucosidase activity; IDA:UniProtKB.
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; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF213; BETA-GLUCOSIDASE 45; 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; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; O80689; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..520
FT                   /note="Beta-glucosidase 45"
FT                   /id="PRO_0000390317"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         52
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         155
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         200..201
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         344
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         417
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         466
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         473..474
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         482
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        220..227
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   DISULFID        352..357
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   520 AA;  59897 MW;  2A165104C966D446 CRC64;
     MKNLTSFVIV ILLQSLLFHV YGRHQSSSKN ILVDSSPFPS DFLFGTASSA YQYEGAFLTD
     GKSLNNWDVF THKNPGKILD KNNADRAVDQ YNRFLEDIQL MSFLGVNSYR FSISWCRILP
     RGRFGEINYL GIKYYNIFID ALISRGIKPF VTLNHVDYPQ ELEDRFQSWL NPEMQKEFGY
     LADICFKHFG NRVKYWTTLN EPNQQLILGY LTGKFPPSRC SSPYGNCSQG NSETEPFIAA
     HNMILAHAKA VNIYKTKYQK EQKGSIGIVV QTSWFEPISD SNADKEAAER AQSFYSNWIL
     DPVIYGKYPK EMVDILGPAL PQFSSNEVKN LEKSRADFVG INHYTSYFIQ DCLTSACNTG
     HGAFKAEGYA LKLDRKGNVT IGELTDVNWQ HIDPTGFHKM LNYLKDRYPN MPMFITENGF
     GDLQKPETTD KELLNDTKRI QYMSGYLEAL QAAMRDGANV KGYFVWSLLD NFEWLFGYKV
     RFGLFHVDLT TLKRSPKQSA SWYKNYIEEH VNRRDIVDNY
//