BGL25_ARATH
ID BGL25_ARATH Reviewed; 531 AA.
AC O82772;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable inactive beta-glucosidase 25;
DE Short=AtBGLU25;
DE Flags: Precursor;
GN Name=BGLU25; Synonyms=GLUC; OrderedLocusNames=At3g03640; ORFNames=T12J13.8;
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 [GENOMIC DNA / MRNA].
RA Gualberto J.M., Schell J., Palme K.;
RT "Beta-glucosidase homolog.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue involved in nucleophilic
CC attack and essential for hydrolase activity. Its enzyme activity is
CC therefore unsure. {ECO:0000305}.
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DR EMBL; AF082157; AAC31962.1; -; mRNA.
DR EMBL; AF082158; AAC32194.1; -; Genomic_DNA.
DR EMBL; AC009327; AAF03468.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73966.1; -; Genomic_DNA.
DR PIR; T51956; T51956.
DR RefSeq; NP_187014.1; NM_111235.4.
DR AlphaFoldDB; O82772; -.
DR SMR; O82772; -.
DR STRING; 3702.AT3G03640.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O82772; -.
DR PRIDE; O82772; -.
DR ProteomicsDB; 240660; -.
DR EnsemblPlants; AT3G03640.1; AT3G03640.1; AT3G03640.
DR GeneID; 821201; -.
DR Gramene; AT3G03640.1; AT3G03640.1; AT3G03640.
DR KEGG; ath:AT3G03640; -.
DR Araport; AT3G03640; -.
DR TAIR; locus:2096449; AT3G03640.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; O82772; -.
DR OMA; THQHSEN; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; O82772; -.
DR BioCyc; ARA:AT3G03640-MON; -.
DR PRO; PR:O82772; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O82772; baseline and differential.
DR Genevisible; O82772; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
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; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..531
FT /note="Probable inactive beta-glucosidase 25"
FT /id="PRO_0000389587"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 477..478
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 222..230
FT /evidence="ECO:0000250"
SQ SEQUENCE 531 AA; 59807 MW; 18EF2E2FDCB7C23B CRC64;
MALKAILFLG LFLVVIVSPI TVYGGAVCPA SSTFGRGSFP DGFLFGATTS AFQHEGAAEE
GGRGSSIWDS FTLKQHSESN NNLDGRLGVD FYHHYKEDVQ LLKKLNMDAF RFSISWSRIF
PHGKKDKGVS ETGVKFYNDL INELIANGVT PLVTLFQWDV PQALEDEYGG FLSDRILEDF
RDFAQFAFNK YGDRVKHWVT INEPYEFSRG GYETGEKAPG RCSKYVNEKC VAGKSGHEVY
TVSHNLLLAH AEAVEEFRKC GKCTGGKIGI VQSPMWFEPY DKKSTSSPSE EIVKRAMDFT
LGWHMEPITH GDYPQAMKDV VGSRLPSFTP EQKEKLKGSY DFVGINYFTS TFVAHTDNVN
PEKPSWEADS RLQLHSNNVD GFKIGSQPAT AKYPVCADGL RKVLKYIKEN YNDPEIIVTG
NGYKETLEEK DVLPDALSDS NRKYYHMRHL MALHGAVCED KVNVKGYFVS SLMDGLEWED
GYKTRSGLYY VDYGHNMGRH EKQSAKWLSK LLEKVPDTIQ SKVDSDSRKE L