ID A0A178MUF6_9PROT Unreviewed; 450 AA.
AC A0A178MUF6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A6A04_00155 {ECO:0000313|EMBL:OAN52394.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN52394.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN52394.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN52394.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAN52394.1}.
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DR EMBL; LWQT01000044; OAN52394.1; -; Genomic_DNA.
DR RefSeq; WP_068490923.1; NZ_LWQT01000044.1.
DR AlphaFoldDB; A0A178MUF6; -.
DR STRING; 1285242.A6A04_00155; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000078428; 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 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000078428}.
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 357
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 411..412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 450 AA; 50285 MW; 401B58B6C377A3F2 CRC64;
MTLAKPEAQA AARQFPKDFF WGASTAAYQI EGAYDTDGRG MTIWDKFTAD GKIMDGSSAK
VACDHYHRYP EDIALMKAAG FNAYRFSLAW PRIIPAGTGA VNPKGLDFYD RLVDKILEAG
IRPMACLYHW DLPQPLEDKG GWQGREIVGP FAEYAAIASK RLGDRVKDWF MLNEPNVVAI
IGYGIGEHAP GYKLGEDGIL KALHHQNLAQ GAALRAIRAE YPKANLGTVI NLQPCRSQDD
DPKNKAAAIR WDAVWNRVPL DGVLRGAIPD VLAEKMAAIV KPGDLEAIKF PLDLLGINYY
SRMTMKHEEG HPFDVFWGDA HCDRWTAMAW PVQPDGLYDL LREFKELYGN PPVFIAENGA
AYDDVVSPDG QVHDSERVAF IRDHVAEVGR ALGDGCNVKG YLVWSLLDNF EWAYGLSKRF
GIVRVDYDTL KRTPKDSYKW FAEVIRTGRV
//
