ID Q8W112_ARATH Unreviewed; 624 AA.
AC Q8W112;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=BGLC1 {ECO:0000313|TAIR:AT5G20950};
GN OrderedLocusNames=At5g20950 {ECO:0000313|Araport:AT5G20950,
GN ECO:0000313|EMBL:AED92910.1};
GN ORFNames=F22D1.120 {ECO:0000313|EMBL:AED92910.1}, F22D1_120
GN {ECO:0000313|EMBL:AED92910.1};
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 {ECO:0000313|EMBL:AAL58902.1};
RN [1] {ECO:0000313|EMBL:AED92910.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|EMBL:AAL58902.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheuk R., Chen H., Kim C.J., Meyers M.C., Banh J., Bowser L., Carninci P.,
RA Chang E., Dale J.M., Goldsmith A.D., Hayashizaki Y., Ishida J., Jones T.,
RA Kamiya A., Karlin-Neumann G., Kawai J., Lam B., Lee J.M., Lin J.,
RA Miranda M., Narusaka M., Nguyen M., Onodera C.S., Palm C.J., Quach H.L.,
RA Sakurai T., Satou M., Seki M., Southwick A., Tang C.C., Toriumi M.,
RA Wu H.C., Yamada K., Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W.,
RA Theologis A., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAM13848.1}
RP NUCLEOTIDE SEQUENCE.
RA Yamada K., Banh J., Chan M.M., Chang C.H., Chang E., Dale J.M., Deng J.M.,
RA Goldsmith A.D., Lee J.M., Onodera C.S., Quach H.L., Tang C., Toriumi M.,
RA Wu H.C., Yamamura Y., Yu G., Bowser L., Carninci P., Chen H., Cheuk R.,
RA Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G.,
RA Kawai J., Kim C., Lam B., Lin J., Meyers M.C., Miranda M., Narusaka M.,
RA Nguyen M., Palm C.J., Sakurai T., Satou M., Seki M., Shinn P.,
RA Southwick A., Shinozaki K., Davis R.W., Ecker J.R., Theologis A.;
RT "Arabidopsis Full Length cDNA Clones.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAN13217.1}
RP NUCLEOTIDE SEQUENCE.
RA Yamada K., Chan M.M., Chang C.H., Dale J.M., Deng J.M., Hsuan V.W.,
RA Lee J.M., Quach H.L., Tang C., Toriumi M., Wallender E.K., Wong C.,
RA Wu H.C., Yu G., Yuan S., Carninci P., Chen H., Cheuk R., Hayashizaki Y.,
RA Ishida J., Jones T., Kamiya A., Kawai J., Kim C.J., Narusaka M., Nguyen M.,
RA Palm C.J., Sakurai T., Satou M., Seki M., Shinn P., Southwick A.,
RA Tripp M.G., Wu T., Shinozaki K., Davis R.W., Ecker J.R., Theologis A.;
RT "Arabidopsis Open Reading Frame (ORF) Clones.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007829|PubMed:17272265}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
RA Maor R., Jones A., Nuhse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6] {ECO:0000313|EMBL:AED92910.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AED92910.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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:0000256|ARBA:ARBA00000448};
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DR EMBL; AF462808; AAL58902.1; -; mRNA.
DR EMBL; AY091027; AAM13848.1; -; mRNA.
DR EMBL; AY142679; AAN13217.1; -; mRNA.
DR EMBL; CP002688; AED92910.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92911.1; -; Genomic_DNA.
DR RefSeq; NP_197595.2; NM_122104.5.
DR RefSeq; NP_851048.1; NM_180717.3.
DR AlphaFoldDB; Q8W112; -.
DR SMR; Q8W112; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR ProteomicsDB; 189169; -.
DR EnsemblPlants; AT5G20950.1; AT5G20950.1; AT5G20950.
DR EnsemblPlants; AT5G20950.2; AT5G20950.2; AT5G20950.
DR GeneID; 832220; -.
DR Gramene; AT5G20950.1; AT5G20950.1; AT5G20950.
DR Gramene; AT5G20950.2; AT5G20950.2; AT5G20950.
DR Araport; AT5G20950; -.
DR TAIR; AT5G20950; BGLC1.
DR HOGENOM; CLU_004542_9_3_1; -.
DR OMA; MYGWDAY; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W112; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 1: Evidence at protein level;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAL58902.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q8W112,
KW ECO:0007829|ProteomicsDB:Q8W112};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..624
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014312383"
FT DOMAIN 45..372
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 409..618
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 624 AA; 67927 MW; 31EC2ECE6A1C1FFE CRC64;
MGTLSKVLCL MLLCCIVAAA EGTLKYKDPK QPLGARIRDL MNRMTLQEKI GQMVQIERSV
ATPEVMKKYF IGSVLSGGGS VPSEKATPET WVNMVNEIQK ASLSTRLGIP MIYGIDAVHG
HNNVYGATIF PHNVGLGVTR DPNLVKRIGA ATALEVRATG IPYAFAPCIA VCRDPRWGRC
YESYSEDYRI VQQMTEIIPG LQGDLPTKRK GVPFVGGKTK VAACAKHFVG DGGTVRGIDE
NNTVIDSKGL FGIHMPGYYN AVNKGVATIM VSYSAWNGLR MHANKELVTG FLKNKLKFRG
FVISDWQGID RITTPPHLNY SYSVYAGISA GIDMIMVPYN YTEFIDEISS QIQKKLIPIS
RIDDALKRIL RVKFTMGLFE EPLADLSFAN QLGSKEHREL AREAVRKSLV LLKNGKTGAK
PLLPLPKKSG KILVAGAHAD NLGYQCGGWT ITWQGLNGND HTVGTTILAA VKNTVAPTTQ
VVYSQNPDAN FVKSGKFDYA IVVVGEPPYA EMFGDTTNLT ISDPGPSIIG NVCGSVKCVV
VVVSGRPVVI QPYVSTIDAL VAAWLPGTEG QGVADALFGD YGFTGKLART WFKSVKQLPM
NVGDRHYDPL YPFGFGLTTK PYKM
//
