BGL32_ARATH
ID BGL32_ARATH Reviewed; 534 AA.
AC Q9FLU8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-glucosidase 32;
DE Short=AtBGLU32;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU32; OrderedLocusNames=At5g24550; ORFNames=K18P6.8;
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010068; BAB11207.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93324.1; -; Genomic_DNA.
DR RefSeq; NP_197843.2; NM_122363.2.
DR AlphaFoldDB; Q9FLU8; -.
DR SMR; Q9FLU8; -.
DR STRING; 3702.AT5G24550.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9FLU8; -.
DR PRIDE; Q9FLU8; -.
DR EnsemblPlants; AT5G24550.1; AT5G24550.1; AT5G24550.
DR GeneID; 832526; -.
DR Gramene; AT5G24550.1; AT5G24550.1; AT5G24550.
DR KEGG; ath:AT5G24550; -.
DR Araport; AT5G24550; -.
DR TAIR; locus:2153944; AT5G24550.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9FLU8; -.
DR OMA; IMNGIKP; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9FLU8; -.
DR BioCyc; ARA:AT5G24550-MON; -.
DR PRO; PR:Q9FLU8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLU8; differential.
DR Genevisible; Q9FLU8; 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 32"
FT /id="PRO_0000389594"
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; 61684 MW; B74495DD8E769475 CRC64;
MAIKLIALVI TICVASWDSA QGRSLRFSTT PLNRYSFPPH FDFGVASSAY QYEGAVEEGG
RSPSIWDNFT HAFPERTNMD NGDVAVDFYH RYKDDIKLIK EMNMDSFRFS LSWSRILPSG
KLSDGVNKEG VQFYKNLIDE LIKNGIKPFV TIYHWDIPQA LDDEYGSFLS PRIIDDFRNF
ARFCFQEFGD KVSMWTTFNE PYVYSVSGYD AGNKAIGRCS KWVNSLCIAG DSGTEPYLVS
HNLLLAHAAA VEEFRKCDKI SQDAKIGIVL SPYWFEPYDI DSESDKEAVE RALVFNIGWH
LSPLVFGDYP ETIKTTAGNR LPSFTKEQSM MLQNSFDFIG INYYTARFVA HDLHVDLSRP
RFTTDQHLQY KLTNRSGDHI SSESDGTKIL WSYPEGLRKL LNYIKNKYNN PTIYITENGF
DDYENGSVTR EEIIEDTKRI EYHQNHLQQL QKAITEDGCN VKGYFTWSLL DNFEWEHGYA
VRFGLYYVDY KNGLSRHAKN SAKWFKHFLQ RSGKPMPLDL FKSVKNWWSA IPMI
