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   27-MAR-2024, entry version 136.
DE   RecName: Full=Beta-glucosidase 44 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU44 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:15604686};
DE   Flags: Precursor;
GN   Name=BGLU44 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At3g18080 {ECO:0000312|Araport:AT3G18080};
GN   ORFNames=MRC8.20 {ECO:0000312|EMBL:BAB02020.1};
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=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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY,
RP   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         Evidence={ECO:0000269|PubMed:15604686};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.43 mM for p-nitrophenyl-beta-D-mannopyranoside
CC         {ECO:0000269|PubMed:15604686};
CC         Vmax=94.7 nmol/sec/mg enzyme with
CC         p-nitrophenyl-beta-D-mannopyranoside as substrate
CC         {ECO:0000269|PubMed:15604686};
CC       pH dependence:
CC         Optimum pH is 4.5. {ECO:0000269|PubMed:15604686};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q75I93, 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.Q9LV33; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9LV33; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT3G18080-1; -.
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; AT3G18080; BGLU44.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9LV33; -.
DR   OMA; VWLKVYP; -.
DR   OrthoDB; 3373839at2759; -.
DR   PhylomeDB; Q9LV33; -.
DR   PRO; PR:Q9LV33; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LV33; baseline and differential.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF28; BETA-GLUCOSIDASE 44; 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; Q9LV33; AT.
PE   1: Evidence at protein 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|UniProtKB:Q7XSK0"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         58
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         159
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         204..205
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         347
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         419
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        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        224..231
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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
//