BGL44_ARATH
ID BGL44_ARATH Reviewed; 512 AA.
AC Q9LV33;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Beta-glucosidase 44;
DE Short=AtBGLU44;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU44; OrderedLocusNames=At3g18080; ORFNames=MRC8.20;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, 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 -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC beta-D-mannoside, cellobiose, 4-methylumbelliferyl-beta-D-glucoside,
CC laminarin, amygdalin, esculin and gentiobiose.
CC {ECO:0000269|PubMed:15604686}.
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 -!- SUBUNIT: Homodimer. Formation of the homodimer is zinc-dependent
CC (Potential). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB020749; BAB02020.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76044.1; -; Genomic_DNA.
DR EMBL; AK316840; BAH19552.1; -; mRNA.
DR EMBL; AK316900; BAH19607.1; -; mRNA.
DR EMBL; AY084864; AAM61427.1; -; mRNA.
DR RefSeq; NP_188436.1; NM_112690.4.
DR AlphaFoldDB; Q9LV33; -.
DR SMR; Q9LV33; -.
DR STRING; 3702.AT3G18080.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9LV33; -.
DR PRIDE; Q9LV33; -.
DR ProteomicsDB; 240424; -.
DR EnsemblPlants; AT3G18080.1; AT3G18080.1; AT3G18080.
DR GeneID; 821333; -.
DR Gramene; AT3G18080.1; AT3G18080.1; AT3G18080.
DR KEGG; ath:AT3G18080; -.
DR Araport; AT3G18080; -.
DR TAIR; locus:2092767; AT3G18080.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9LV33; -.
DR OMA; WHVCEHG; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9LV33; -.
DR PRO; PR:Q9LV33; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV33; baseline and differential.
DR Genevisible; Q9LV33; AT.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0080081; F:4-methylumbelliferyl-beta-D-glucopyranoside beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0047668; F:amygdalin beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0080083; F:beta-gentiobiose beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IDA:TAIR.
DR GO; GO:0080082; F:esculin beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..512
FT /note="Beta-glucosidase 44"
FT /id="PRO_0000383462"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 419
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347
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 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..231
FT /evidence="ECO:0000250"
SQ SEQUENCE 512 AA; 58983 MW; A870F9BB20C342E7 CRC64;
MRHLSSPPWP LLLLLLLSSF TSGESSLSAE KNKLHTGGLS RQSFPKGFVF GTATSAYQVE
GETHQDGRGP SIWDAFVKIP GKIAKNATAE ITVDQYHRYK EDVDLMKKLN FDAYRFSISW
SRIFPEGSGK VNWKGVAYYN RLIDYMVQKG ITPYANLYHY DLPLALENKY KGLLGRQVVK
DFADYAEFCY KTFGDRVKNW MTFNEPRVVA ALGYDNGIFA PGRCSKAFGN CTEGNSATEP
YIVTHHLILA HAAAVQRYRK YYQAKQKGRV GILLDFVWYE PLTRSKADNL AAQRARDFHI
GWFIHPLVYG EYPKTMQNIV KERLPKFTEK EVKMVKGSID FVGINQYTTY YMSEPHPTTK
PKDLGYQQDW NVEFGFAKLG KPIGPRAYSS WLYNVPWGMY KALMYMKERY GNPTMILSEN
GMDDPGNVTL AQGLHDTTRI KYYKDYLTNL KKARDDGANV VGYFAWSLLD NFEWLSGYTS
RFGIVYVDYK TLKRYPKMSA QWFKQLLKRN NK
