BGL45_ARATH
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 03-AUG-2022, entry version 130.
DE RecName: Full=Beta-glucosidase 45;
DE Short=AtBGLU45;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU45; OrderedLocusNames=At1g61810; ORFNames=F8K4.2, 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, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE 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 -!- 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.AT1G61810.3; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O80689; -.
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 eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; O80689; -.
DR OMA; KWMQWNY; -.
DR PhylomeDB; O80689; -.
DR BioCyc; ARA:AT1G61810-MON; -.
DR SABIO-RK; O80689; -.
DR PRO; PR:O80689; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80689; baseline and differential.
DR Genevisible; O80689; AT.
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 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; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
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"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 473..474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 220..227
FT /evidence="ECO:0000250"
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
