BGL24_ARATH
ID BGL24_ARATH Reviewed; 533 AA.
AC Q9LKR7;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Beta-glucosidase 24;
DE Short=AtBGLU24;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU24; OrderedLocusNames=At5g28510; ORFNames=T26D3.6;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF88017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF262043; AAF88017.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93809.1; -; Genomic_DNA.
DR RefSeq; NP_198203.1; NM_122734.2.
DR AlphaFoldDB; Q9LKR7; -.
DR SMR; Q9LKR7; -.
DR STRING; 3702.AT5G28510.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9LKR7; -.
DR PRIDE; Q9LKR7; -.
DR ProteomicsDB; 240681; -.
DR EnsemblPlants; AT5G28510.1; AT5G28510.1; AT5G28510.
DR GeneID; 832944; -.
DR Gramene; AT5G28510.1; AT5G28510.1; AT5G28510.
DR KEGG; ath:AT5G28510; -.
DR Araport; AT5G28510; -.
DR TAIR; locus:2182768; AT5G28510.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9LKR7; -.
DR OMA; IIMENGY; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9LKR7; -.
DR BioCyc; ARA:AT5G28510-MON; -.
DR PRO; PR:Q9LKR7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKR7; baseline and differential.
DR Genevisible; Q9LKR7; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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; PS00014; ER_TARGET; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..533
FT /note="Beta-glucosidase 24"
FT /id="PRO_0000389586"
FT MOTIF 530..533
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484..485
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..239
FT /evidence="ECO:0000250"
SQ SEQUENCE 533 AA; 61034 MW; 062E9D4C144E4884 CRC64;
MVLQKLPLMS IGLLWLLIIV GPLVNADGPV CPPKPSDKLS RAHFPKGFLF GTATAAYQVE
GAVNETCRGP SVWDIYCKKY PEKCNGDNGT QAVDFFYRYK EDIQLMKNLN TDSFRLSISW
TRIFPHGREE NGVSKSGVQF YHDLIDELKR NGIIPFVTVF HWDTPQTLEN EYGGFLSAHI
VKDFREYAEF VFKEYGGKVK HWITFNEPWV FAHAGYDVGK KAPGRCSPYA KDETVKGDCL
GGRSGYEAYL VSHNLLNAHA EAVEAFRQCE KCKGGKIGIA HSPAWFEPHD FKDEQSGATI
DRALDFIMGW HLDTTMFGDY PQTMKDIVGH RLPKFTTEQI AKLKNSADFV GINYYTSTFS
KHLEKPNHAE PKFKQDSLVE WKNKNVNNIT IGSKPETGPL PVYSTGFRKV LKYVKDKYAN
PEIIIMENGY GENLKENDSV ENGTADYNRE SYLKKHLWSM HKAICEDKVN VTGYFVWSLM
DNFEWQDGFK NRFGLYYIDY KNNLTRHEKV SGKYYREFLS EGVRPSAIKK DEL
