BGL31_ARATH
ID BGL31_ARATH Reviewed; 534 AA.
AC Q9FLU9;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Beta-glucosidase 31;
DE Short=AtBGLU31;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU31; OrderedLocusNames=At5g24540; ORFNames=K18P6.7;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB010068; BAB11206.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93323.1; -; Genomic_DNA.
DR EMBL; DQ446980; ABE66178.1; -; mRNA.
DR RefSeq; NP_197842.1; NM_122362.2.
DR AlphaFoldDB; Q9FLU9; -.
DR SMR; Q9FLU9; -.
DR STRING; 3702.AT5G24540.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9FLU9; -.
DR PRIDE; Q9FLU9; -.
DR EnsemblPlants; AT5G24540.1; AT5G24540.1; AT5G24540.
DR GeneID; 832525; -.
DR Gramene; AT5G24540.1; AT5G24540.1; AT5G24540.
DR KEGG; ath:AT5G24540; -.
DR Araport; AT5G24540; -.
DR TAIR; locus:2153934; AT5G24540.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9FLU9; -.
DR OMA; MSCAISK; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9FLU9; -.
DR BioCyc; ARA:AT5G24540-MON; -.
DR PRO; PR:Q9FLU9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLU9; baseline and differential.
DR Genevisible; Q9FLU9; AT.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
DR InterPro; IPR001360; Glyco_hydro_1.
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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..534
FT /note="Beta-glucosidase 31"
FT /id="PRO_0000389593"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 474..475
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219..227
FT /evidence="ECO:0000250"
SQ SEQUENCE 534 AA; 61872 MW; 715CD0BB48EB8DCA CRC64;
MAIKLIALVI TLCVASWDVA QGRSLRFSTT PLNRYSFPPH FDFGVASSAY QYEGAVEEGG
RSLSIWDNFT HAFPERTNMD NGDVAVDFYH RYKEDIKLIK EMNMDSFRFS LSWSRILPSG
KLSDGVNKEG VQFYKNLIDE LIENGIKPFV TIYHWDIPQA LDDEYGSFLS PRIIDDFRNY
ARFCFQEFGD KVSMWTTFNE PYVYSVSGYD AGNKAMGRCS KWVNSLCIAG DSGTEPYLVS
HHLLLAHAAA VEEFRKCDKI SQDSKIGIVL SPYWFEPYDS ASNADKEAVE RALAFNIGWH
LSPLVFGDYP ETIKISAGNR LPSFTKEQSM MVKNSFDFIG VNYYTARFVA HDLNVDISRP
RFMTDQHLQY KLTNRTGDTI SLESDGTKIL WSYPEGLRKI LNYIKNKYNN PTIYITENGF
DDYENGTVTR EEILEDTKRI EYHQKHLQEL QKAITEDGCD VKGYFTWSLL DNFEWEHGYA
VRFGLYYVDY KNGLQRHAKH SAMWFKHFLE RSGKPMPMDL FKSVKRWWST LQMI
