BGL30_ARATH
ID BGL30_ARATH Reviewed; 577 AA.
AC Q9M1C9; Q39225; Q39226; Q8L7I3; Q9ASR7; Q9FVM4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-glucosidase 30;
DE Short=AtBGLU30;
DE EC=3.2.1.21;
DE AltName: Full=Protein DARK INDUCIBLE 2;
DE AltName: Full=Protein SENESCENCE-RELATED GENE 2;
DE Flags: Precursor;
GN Name=BGLU30; Synonyms=DIN2, SRG2; OrderedLocusNames=At3g60140;
GN ORFNames=T2O9.120;
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 [MRNA], AND INDUCTION.
RX PubMed=11080291; DOI=10.1104/pp.124.3.1139;
RA Fujiki Y., Ito M., Nishida I., Watanabe A.;
RT "Multiple signaling pathways in gene expression during sugar starvation.
RT Pharmacological analysis of din gene expression in suspension-cultured
RT cells of Arabidopsis.";
RL Plant Physiol. 124:1139-1148(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-88 AND 456-504.
RX PubMed=8883383; DOI=10.1104/pp.112.2.705;
RA Callard D., Axelos M., Mazzolini L.;
RT "Novel molecular markers for late phases of the growth cycle of Arabidopsis
RT thaliana cell-suspension cultures are expressed during organ senescence.";
RL Plant Physiol. 112:705-715(1996).
RN [6]
RP INDUCTION.
RX PubMed=11240919; DOI=10.1034/j.1399-3054.2001.1110312.x;
RA Fujiki Y., Yoshikawa Y., Sato T., Inada N., Ito M., Nishida I.,
RA Watanabe A.;
RT "Dark-inducible genes from Arabidopsis thaliana are associated with leaf
RT senescence and repressed by sugars.";
RL Physiol. Plantarum 111:345-352(2001).
RN [7]
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 -!- INDUCTION: By sucrose starvation, dark and senescence.
CC {ECO:0000269|PubMed:11080291, ECO:0000269|PubMed:11240919}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK32907.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAM91436.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF159376; AAG23719.1; -; mRNA.
DR EMBL; AL138658; CAB75929.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80017.1; -; Genomic_DNA.
DR EMBL; AF367320; AAK32907.1; ALT_SEQ; mRNA.
DR EMBL; AY133606; AAM91436.1; ALT_SEQ; mRNA.
DR EMBL; X82623; CAA57943.1; -; mRNA.
DR EMBL; X82624; CAA57944.1; -; mRNA.
DR PIR; T47838; T47838.
DR RefSeq; NP_191573.1; NM_115877.4.
DR AlphaFoldDB; Q9M1C9; -.
DR SMR; Q9M1C9; -.
DR STRING; 3702.AT3G60140.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR MetOSite; Q9M1C9; -.
DR PaxDb; Q9M1C9; -.
DR PRIDE; Q9M1C9; -.
DR ProteomicsDB; 240764; -.
DR EnsemblPlants; AT3G60140.1; AT3G60140.1; AT3G60140.
DR GeneID; 825184; -.
DR Gramene; AT3G60140.1; AT3G60140.1; AT3G60140.
DR KEGG; ath:AT3G60140; -.
DR Araport; AT3G60140; -.
DR TAIR; locus:2101427; AT3G60140.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9M1C9; -.
DR OMA; INSKEYP; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9M1C9; -.
DR BioCyc; ARA:AT3G60140-MON; -.
DR PRO; PR:Q9M1C9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1C9; baseline and differential.
DR Genevisible; Q9M1C9; 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 Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..577
FT /note="Beta-glucosidase 30"
FT /id="PRO_0000389592"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 410
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 467..468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213..221
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="E -> K (in Ref. 1; AAG23719)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..66
FT /note="SLT -> TLS (in Ref. 4; AAK32907)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="D -> G (in Ref. 4; AAK32907/AAM91436)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="S -> A (in Ref. 4; AAK32907)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="S -> R (in Ref. 4; AAK32907)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="F -> I (in Ref. 4; AAK32907)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> R (in Ref. 4; AAK32907/AAM91436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 66920 MW; BAD5112154DB1E11 CRC64;
MAKGSWFFII LFIISMLENM INSLELDRHS FPDDFIFGTA ASAFQYEGAT SEGGKSPTIW
DHFSLTYPER TKMHNADVAI DFYHRYKDDI KLMKELNMDA FRFSISWSRL IPSGKLKDGV
NKEGVQFYKD LIDELLANDI QPSMTLYHWD HPQSLEDEYG GFLSPKIVED FRDFARICFE
EFGDKVKMWT TINEPYIMTV AGYDQGNKAA GRCSKWVNEK CQAGDSSTEP YIVSHHTLLA
HAAAVEEFRK CEKTSHDGQI GIVLSPRWFE PYHSDSTDDK EAAERALAFE IGWHLDPVIH
GDYPEIVKKY AGNKLPSFTV EQSKMLQNSS DFVGINYYTA RFAAHLPHID PEKPRFKTDH
HVEWKLTNHS GHIIGPGEER GFLFSHPEGL RKVLNYIKER YNNMPVYIKE NGINDNDDGT
KPREEIVKDT FRIEYHKTHF EELHKAIVED GCDVRGYYAW SLMDNFEWEH GYTARFGLYY
VDFVNGLKRY PKDSVKWFKR FLKKSVVGES NKEEVEEMSR AEGNKTFKGF EESAGFFASF
MAMNQSRRDE ENNRCSFDFP HTHFGVLQGI ENPSSFY
