BGL27_ARATH
ID BGL27_ARATH Reviewed; 540 AA.
AC Q9M1D1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-glucosidase 27;
DE Short=AtBGLU27;
DE EC=3.2.1.21;
GN Name=BGLU27; OrderedLocusNames=At3g60120; ORFNames=T2O9.100;
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=CAB75927.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138658; CAB75927.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80013.1; -; Genomic_DNA.
DR PIR; T47836; T47836.
DR RefSeq; NP_191571.4; NM_115875.5.
DR AlphaFoldDB; Q9M1D1; -.
DR SMR; Q9M1D1; -.
DR STRING; 3702.AT3G60120.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9M1D1; -.
DR PRIDE; Q9M1D1; -.
DR EnsemblPlants; AT3G60120.1; AT3G60120.1; AT3G60120.
DR GeneID; 825182; -.
DR Gramene; AT3G60120.1; AT3G60120.1; AT3G60120.
DR KEGG; ath:AT3G60120; -.
DR Araport; AT3G60120; -.
DR TAIR; locus:2101407; AT3G60120.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9M1D1; -.
DR OMA; HIWNESE; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9M1D1; -.
DR BioCyc; ARA:AT3G60120-MON; -.
DR PRO; PR:Q9M1D1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1D1; baseline and differential.
DR Genevisible; Q9M1D1; 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: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 Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..540
FT /note="Beta-glucosidase 27"
FT /id="PRO_0000389589"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 397
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 454..455
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 540 AA; 62450 MW; 7FC4593693AEA940 CRC64;
MTQRKNMYSK KNSFGRSDFP EGFLFGTASS AYQYEGARNE APRGESVWDT FVRKYPERNC
YSNADQAIEF YNHYKDDIQR MKDINMDAFR FSISWPRIFP LGKKSKGVNK EGIQFYNDLI
DELLANGITP LATLFHWDTP QALEDEYSGF LSEEAVDDFK DFAALCFEEF GDRVKLWVTL
NEPWVYSIGG YDTGRKAPGR ASKYMNEAAV AGESGLEVYT VSHNLLLAHA EAVEVFRNNP
KCKDGKIGIA HCPVWFEPYD SNCPKDIEAC ERAMEFMFGW HMDPTVYGDY PAVMKKSIGK
RLPSFTAAQS KKLRGSFDFV GVNYYSAFYV KNIDEVNHDK PNWRSDARIE WRKENNAGQT
LGVRGGSEWD FLYPQGLRKF LNYAKNKYES PKFMITENGH CDIDYEKKPK LSNLMDLQRT
EYHKKHLQSI QQAIQEDGVV VEGYFAWSLL DNCEWNAGYG VRYGLFYVDY NNGLKRFPKM
SAMWFKEFLK REEEIEDSEE EEYVLKSTMN KKRFLLATGS SASCFIPKMS ESSKALELLF
