BGL16_ARATH
ID BGL16_ARATH Reviewed; 514 AA.
AC Q9M1D0; Q9CAZ8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Beta-glucosidase 16;
DE Short=AtBGLU16;
DE EC=3.2.1.21;
DE AltName: Full=Protein YELLOW-LEAF-SPECIFIC GENE 1;
DE Flags: Precursor;
GN Name=BGLU16; Synonyms=YLS1; OrderedLocusNames=At3g60130; ORFNames=T2O9.110;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 315-510 (ISOFORM 1), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Leaf;
RX PubMed=11230571; DOI=10.1093/pcp/pce021;
RA Yoshida S., Ito M., Nishida I., Watanabe A.;
RT "Isolation and RNA gel blot analysis of genes that could serve as potential
RT molecular markers for leaf senescence in Arabidopsis thaliana.";
RL Plant Cell Physiol. 42:170-178(2001).
RN [5]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M1D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M1D0-2; Sequence=VSP_038455;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in cauline leaves and
CC flowers. {ECO:0000269|PubMed:11230571}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in leaves during natural senescence.
CC {ECO:0000269|PubMed:11230571}.
CC -!- INDUCTION: By abscisic acid (ABA) and dark.
CC {ECO:0000269|PubMed:11230571}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AL138658; CAB75928.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80014.1; -; Genomic_DNA.
DR EMBL; AY045953; AAK76627.1; -; mRNA.
DR EMBL; AY113935; AAM44983.1; -; mRNA.
DR EMBL; AB047804; BAB32881.1; -; mRNA.
DR PIR; T47837; T47837.
DR RefSeq; NP_191572.1; NM_115876.5. [Q9M1D0-1]
DR AlphaFoldDB; Q9M1D0; -.
DR SMR; Q9M1D0; -.
DR BioGRID; 10497; 1.
DR IntAct; Q9M1D0; 1.
DR STRING; 3702.AT3G60130.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9M1D0; -.
DR PRIDE; Q9M1D0; -.
DR ProteomicsDB; 240686; -. [Q9M1D0-1]
DR EnsemblPlants; AT3G60130.1; AT3G60130.1; AT3G60130. [Q9M1D0-1]
DR GeneID; 825183; -.
DR Gramene; AT3G60130.1; AT3G60130.1; AT3G60130. [Q9M1D0-1]
DR KEGG; ath:AT3G60130; -.
DR Araport; AT3G60130; -.
DR TAIR; locus:2101417; AT3G60130.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9M1D0; -.
DR OMA; EGYTIGE; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9M1D0; -.
DR BioCyc; ARA:AT3G60130-MON; -.
DR PRO; PR:Q9M1D0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1D0; baseline and differential.
DR Genevisible; Q9M1D0; 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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..514
FT /note="Beta-glucosidase 16"
FT /id="PRO_0000389579"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 465..466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 218..226
FT /evidence="ECO:0000250"
FT VAR_SEQ 381..391
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038455"
SQ SEQUENCE 514 AA; 58043 MW; ED42E2FC638FDB6D CRC64;
MRGKFLSLLL LITLACIGVS AKKHSTRPRL RRNDFPQDFV FGSATSAYQC EGAAHEDGRG
PSIWDSFSEK FPEKIMDGSN GSIADDSYNL YKEDVNLLHQ IGFDAYRFSI SWSRILPRGT
LKGGINQAGI EYYNNLINQL ISKGVKPFVT LFHWDLPDAL ENAYGGLLGD EFVNDFRDYA
ELCFQKFGDR VKQWTTLNEP YTMVHEGYIT GQKAPGRCSN FYKPDCLGGD AATEPYIVGH
NLLLAHGVAV KVYREKYQAT QKGEIGIALN TAWHYPYSDS YADRLAATRA TAFTFDYFME
PIVYGRYPIE MVSHVKDGRL PTFTPEESEM LKGSYDFIGV NYYSSLYAKD VPCATENITM
TTDSCVSLVG ERNGVPIGPA AGSDWLLIYP KGIRDLLLHA KFRYNDPVLY ITENGVDEAN
IGKIFLNDDL RIDYYAHHLK MVSDAISIGV NVKGYFAWSL MDNFEWSEGY TVRFGLVFVD
FEDGRKRYLK KSAKWFRRLL KGAHGGTNEQ VAVI
