ID J2VR00_9BRAD Unreviewed; 486 AA.
AC J2VR00;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN ORFNames=PMI42_07207 {ECO:0000313|EMBL:EJN08597.1};
OS Bradyrhizobium sp. YR681.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN08597.1, ECO:0000313|Proteomes:UP000007272};
RN [1] {ECO:0000313|EMBL:EJN08597.1, ECO:0000313|Proteomes:UP000007272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR681 {ECO:0000313|EMBL:EJN08597.1,
RC ECO:0000313|Proteomes:UP000007272};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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,
CC ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU361175}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJN08597.1}.
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DR EMBL; AKIY01000298; EJN08597.1; -; Genomic_DNA.
DR RefSeq; WP_008142957.1; NZ_AKIY01000298.1.
DR AlphaFoldDB; J2VR00; -.
DR PATRIC; fig|1144344.3.peg.6589; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000007272; Unassembled WGS sequence.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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 PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..486
FT /note="Beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003756953"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 445..446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 486 AA; 53585 MW; 77FDE10EDCF8925A CRC64;
MFAKFSRRDF ARFAGLAALG AASGARAAAD AAADRHAPAA FPKDFLWGTA TSSYQIEGAV
NEDGRGKSIW DTFSHTPGKI EDGSTGDRAN EHYRRYREDV ALIKALGVRA YRFSIAWPRV
FPEGTGQPNP KGLDFYDRLV DELLANGIEP CATLYHWDLP QALQDRVGGW QSSDTSKAFA
DYAAHVATRL TDRVKTIFTV NEVGRFLNFG YGWGIDAPGL KLPTAQLNQA RHHVALAHGL
AVQAIRASGR AGTRVGAAEN IAACVPAIAT PENIRAAEIA TRELNAGFLG VVLEGKYTDG
YLAYAGADAP KFTPDELKII GAPNDFVGLN IYAPQFYVTA SDRAPGFHVL PFPTSFPHMN
SEWLRVGPEV IYWAPRLAAK IWNIETIYIS ENGTSSDDKI AADGQVYDLD RIMFLRNYLT
QMQRATAEGV PIRGYFLWSL MDNFEWIFGY GKRFGLYRVD FETQARVPKL SAAFYRDVVM
RNAIGV
//
