BGL29_ARATH
ID BGL29_ARATH Reviewed; 590 AA.
AC Q8GXT2; A8MQN1; O64881;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Beta-glucosidase 29;
DE Short=AtBGLU29;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU29; OrderedLocusNames=At2g44470; ORFNames=F4I1.28;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 -!- 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=3;
CC Name=1;
CC IsoId=Q8GXT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GXT2-2; Sequence=VSP_038462, VSP_038463;
CC Name=3;
CC IsoId=Q8GXT2-3; Sequence=VSP_038460, VSP_038461;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC16093.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004521; AAC16093.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10423.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10424.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10425.1; -; Genomic_DNA.
DR EMBL; AK118055; BAC42686.1; -; mRNA.
DR PIR; T02402; T02402.
DR RefSeq; NP_001078056.1; NM_001084587.1. [Q8GXT2-3]
DR RefSeq; NP_001118524.1; NM_001125052.1. [Q8GXT2-1]
DR RefSeq; NP_850417.1; NM_180086.1. [Q8GXT2-2]
DR AlphaFoldDB; Q8GXT2; -.
DR SMR; Q8GXT2; -.
DR STRING; 3702.AT2G44470.3; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q8GXT2; -.
DR PRIDE; Q8GXT2; -.
DR ProteomicsDB; 240420; -. [Q8GXT2-1]
DR EnsemblPlants; AT2G44470.1; AT2G44470.1; AT2G44470. [Q8GXT2-2]
DR EnsemblPlants; AT2G44470.2; AT2G44470.2; AT2G44470. [Q8GXT2-3]
DR EnsemblPlants; AT2G44470.3; AT2G44470.3; AT2G44470. [Q8GXT2-1]
DR GeneID; 819054; -.
DR Gramene; AT2G44470.1; AT2G44470.1; AT2G44470. [Q8GXT2-2]
DR Gramene; AT2G44470.2; AT2G44470.2; AT2G44470. [Q8GXT2-3]
DR Gramene; AT2G44470.3; AT2G44470.3; AT2G44470. [Q8GXT2-1]
DR KEGG; ath:AT2G44470; -.
DR Araport; AT2G44470; -.
DR TAIR; locus:2050497; AT2G44470.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q8GXT2; -.
DR OMA; ARAMSWN; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q8GXT2; -.
DR BioCyc; ARA:AT2G44470-MON; -.
DR PRO; PR:Q8GXT2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GXT2; baseline and differential.
DR Genevisible; Q8GXT2; 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..590
FT /note="Beta-glucosidase 29"
FT /id="PRO_0000389591"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 470..471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 216..224
FT /evidence="ECO:0000250"
FT VAR_SEQ 381..397
FT /note="DDRGKIHSHPEGLRRVL -> VCNILIIFIPKILKCFD (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038460"
FT VAR_SEQ 398..590
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038461"
FT VAR_SEQ 451
FT /note="I -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_038462"
FT VAR_SEQ 452..590
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_038463"
SQ SEQUENCE 590 AA; 68244 MW; D0854736ED5FC6E2 CRC64;
MNVQIFILLL IISWLTPKIT SLPPESQVLD RSSFPDDFVF GTAISAFQSE GATSEGGKSP
TIWDYFSHTF PERTNMQNAD VAVDFYHRYK DDIKLIEELN VDAFRFSISW ARLIPSGKVK
DGVNKEGVQF YKALIDELIA NGIQPSVTLY HWDHPQALED EYGGFLNPQI IEDFRNFARV
CFENFGDKVK MWTTINEPYV ISVAGYDTGI KAVGRCSKWV NSRCQAGDSA IEPYIVSHHL
LLSHAAAVQE FRNCNKTLQD GKIGIVISPW WLEPYDSTSS ADKEAVERGL PLELEWHLNP
VIYGDYPETM KKHVGNRLPA FTPEQSKMLI NSSDFIGVNY YSIHFTAHLP HIDHTRPRFR
TDHHFEKKLI NRSNHETGPG DDRGKIHSHP EGLRRVLNYI KDKYNNPIVY VKENGIDHYD
DGTKSRETIL KDTFRISYHQ DHLKQVHKAI IEDGCDVRGY YVWSLFDNFE WEHGYNSRFG
MYYVDFKNNL QRYPKDSVNW FKKFLSRPVV RSEETEDEKV CNVSRKEEKI NKALDVSEGF
KTSVDSIVNL IKNGSRIEEE DDEEERDFCA FKNHNDQLGF FLKLQNSLGF
