BGL12_ARATH
ID BGL12_ARATH Reviewed; 507 AA.
AC Q9FH03;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Beta-glucosidase 12;
DE Short=AtBGLU12;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU12; OrderedLocusNames=At5g42260; ORFNames=K5J14.7;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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; AB023032; BAB10199.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94789.1; -; Genomic_DNA.
DR EMBL; DQ056704; AAY78850.1; -; mRNA.
DR RefSeq; NP_199041.1; NM_123591.2.
DR AlphaFoldDB; Q9FH03; -.
DR SMR; Q9FH03; -.
DR STRING; 3702.AT5G42260.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9FH03; -.
DR PRIDE; Q9FH03; -.
DR EnsemblPlants; AT5G42260.1; AT5G42260.1; AT5G42260.
DR GeneID; 834231; -.
DR Gramene; AT5G42260.1; AT5G42260.1; AT5G42260.
DR KEGG; ath:AT5G42260; -.
DR Araport; AT5G42260; -.
DR TAIR; locus:2157632; AT5G42260.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR OMA; RIDYFSH; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9FH03; -.
DR BioCyc; ARA:AT5G42260-MON; -.
DR PRO; PR:Q9FH03; -.
DR Proteomes; UP000006548; Chromosome 5.
DR Genevisible; Q9FH03; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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: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..507
FT /note="Beta-glucosidase 12"
FT /id="PRO_0000389575"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 50
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 459
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
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 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219..227
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 56966 MW; 7F7197A3D50D45C4 CRC64;
MRTIYLSLLV FIIVLALNEV MAKKHSSTPK LRRSDFPEDF IFGAATSAYQ VEGAAHEDGR
GPSIWDTFSE KYPEKIKDGS NGSIASDSYH LYKEDVGLLH QIGFDAYRFS ISWSRILPRE
NLKGGINQAG IDYYNNLINE LLSKGIKPFA TIFHWDTPQS LEDAYGGFLG AEIVNDFRDY
ADICFKNFGD RVKHWMTLNE PLTVVQQGYV AGVMAPGRCS KFTNPNCTAG NGATEPYIVG
HNLILAHGEA VKVYREKYKA SQKGQVGIAL NAGWNLPYSE SAEDRLAAAR AMAFTFDYFM
EPLVTGKYPI DMVNYVKGGR LPTFTAKQSK MLKGSYDFIG RNYYSSSYAK DVPCSSENVT
LFSDPCASVT GEREGVPIGP KAASDWLLIY PKGIRDLLLY AKYKFKDPVM YITENGRDEA
STGKIDLKDS ERIDYYAQHL KMVQDAISIG ANVKGFFAWS LLDNFEWATG YAVRFGLVYV
DFNGGRKRYP KKSAKWFKKL LNEKKKN
