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   27-MAR-2024, entry version 128.
DE   RecName: Full=Beta-glucosidase 29 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU29 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE   Flags: Precursor;
GN   Name=BGLU29 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At2g44470 {ECO:0000312|Araport:AT2G44470};
GN   ORFNames=F4I1.28 {ECO:0000312|EMBL:AAC16093.1};
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         Evidence={ECO:0000250|UniProtKB:O64879};
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.Q8GXT2; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q8GXT2; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT2G44470-3; -.
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; AT2G44470; BGLU29.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q8GXT2; -.
DR   OMA; DEEQNRC; -.
DR   OrthoDB; 640576at2759; -.
DR   PhylomeDB; Q8GXT2; -.
DR   BioCyc; ARA:AT2G44470-MONOMER; -.
DR   PRO; PR:Q8GXT2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8GXT2; baseline and differential.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF176; BETA-GLUCOSIDASE 29; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; Q8GXT2; AT.
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|UniProtKB:Q7XSK0"
FT   ACT_SITE        413
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         48
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         151
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         196..197
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         341
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         413
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         463
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         470..471
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         479
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        216..224
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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
//