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Database: UniProt
Entry: A0XZR8_9GAMM
LinkDB: A0XZR8_9GAMM
Original site: A0XZR8_9GAMM 
ID   A0XZR8_9GAMM            Unreviewed;       442 AA.
AC   A0XZR8;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=ATW7_07854 {ECO:0000313|EMBL:EAW28483.1};
OS   Alteromonadales bacterium TW-7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=156578 {ECO:0000313|EMBL:EAW28483.1, ECO:0000313|Proteomes:UP000004833};
RN   [1] {ECO:0000313|EMBL:EAW28483.1, ECO:0000313|Proteomes:UP000004833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-7 {ECO:0000313|EMBL:EAW28483.1,
RC   ECO:0000313|Proteomes:UP000004833};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (DEC-2006) 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|ARBA:ARBA00010838, 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:EAW28483.1}.
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DR   EMBL; AAVS01000006; EAW28483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0XZR8; -.
DR   eggNOG; COG2723; Bacteria.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000004833; 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; IPR018120; Glyco_hydro_1_AS.
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; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|RuleBase:RU361175};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}.
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        352
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10055"
FT   BINDING         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         405..406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   442 AA;  50027 MW;  C18519324EF91BD1 CRC64;
     MTKISLPTCS PLLTKEFIYG VATASFQIEG GSTHRLPCIW DTFCDTPGKI ADNSNGHVAC
     DHYNNWKKDI DLIESLGVDA YRLSISWPRV ITKSGELNPE GVKFYTDILD ELKKRNIKAF
     VTLYHWDLPQ HLEDEGGWLN RETAYAFAHY VDLITLAFGD RVHSYATLNE PFCSAFLGYE
     IGIHAPGKVG KQYGRKAAHH LLLAHGLAMT VLKQNSPTTL NGIVLNFTPC YSISEDADDI
     AATAFADDYL NQWYMKPIMD GTYPAIIEQL PSTHLPDIHD DDMAIISQSI DYLGINFYTR
     QFYKAHPTEI YEPIEPTGPL TDMGWEIYPK SFTELLVTLN NTYNLPPIFI TENGAAMPDS
     YNNGEINDVD RLDYYNSHLN AVHNATEQGV RIDGYFAWSL MDNFEWAEGY LKRFGIVYVD
     YSTQQRTIKN SGLAYKALIS NR
//
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