BGL07_ARATH
ID BGL07_ARATH Reviewed; 502 AA.
AC Q9LZJ1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Beta-glucosidase 7;
DE Short=AtBGLU7;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU7; OrderedLocusNames=At3g62740; ORFNames=F26K9.170;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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=CAB83124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162651; CAB83124.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80386.1; -; Genomic_DNA.
DR PIR; T48063; T48063.
DR RefSeq; NP_191833.2; NM_116139.3.
DR AlphaFoldDB; Q9LZJ1; -.
DR SMR; Q9LZJ1; -.
DR STRING; 3702.AT3G62740.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9LZJ1; -.
DR PRIDE; Q9LZJ1; -.
DR ProteomicsDB; 240782; -.
DR EnsemblPlants; AT3G62740.1; AT3G62740.1; AT3G62740.
DR GeneID; 825449; -.
DR Gramene; AT3G62740.1; AT3G62740.1; AT3G62740.
DR KEGG; ath:AT3G62740; -.
DR Araport; AT3G62740; -.
DR TAIR; locus:2081665; AT3G62740.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9LZJ1; -.
DR OMA; APIRVEM; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; Q9LZJ1; -.
DR BioCyc; ARA:AT3G62740-MON; -.
DR PRO; PR:Q9LZJ1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZJ1; baseline and differential.
DR Genevisible; Q9LZJ1; 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 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 Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..502
FT /note="Beta-glucosidase 7"
FT /id="PRO_0000389569"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 392
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 442..443
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 502 AA; 56418 MW; 558B983EB2458FF9 CRC64;
MKPFSQFFVF VVTVSATSYI DAFTRNDFPN DFLFGAATSA YQWEGAFDED GKSPSVWDTT
SHCDSGSNNG DIACDGYHKY KEDVMLMAEM GLESFRFSIS WSRLIPNGRG RINPKGLLFY
KNLIKELRSH GIEPQVTLYH YDLPQSLEDE YGGWINRKII EDFTAFADVC FREFGEDVKL
WTKINEATLF AIGSYGDGMR YGHCPPMNYS TANVCTETYI AGHNMLLAHS SASNLYKLKY
KTKQRGSVGL SIYAYGLSPY TDSKDDETAT ERAEAFLFGW MLKPLVVGDY PDIMKRTLGS
RLPVFSEEES KQVKGSSDFV GVVHYNTFYV TNRPAPSLVT SINKLFFADI GAYLIAAGNA
SLFEFDAVPW GLEGILQHIK QSYNNPPIYI LENGKPMKHG STLQDTPRAE FIQAYIGAVH
NAITNGSDTR GYFVWSMIDL YELIGRYMTS YGMYYVNFSD PGRKRSPKLS ASWYTGFLNG
TIDVASQDTI QLQRKCSGSS SL
