ID A0A1X7PZ56_9RHOB Unreviewed; 442 AA.
AC A0A1X7PZ56;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=SAMN05661107_3328 {ECO:0000313|EMBL:SMH56944.1};
OS Maritimibacter sp. HL-12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=1162418 {ECO:0000313|EMBL:SMH56944.1, ECO:0000313|Proteomes:UP000193836};
RN [1] {ECO:0000313|EMBL:SMH56944.1, ECO:0000313|Proteomes:UP000193836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-12 {ECO:0000313|EMBL:SMH56944.1,
RC ECO:0000313|Proteomes:UP000193836};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU361175}.
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DR EMBL; FXBQ01000001; SMH56944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7PZ56; -.
DR STRING; 1162418.SAMN05661107_3328; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000193836; 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; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000193836}.
FT ACT_SITE 168
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 BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 295
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; 48844 MW; CB2B653FCBAD82E1 CRC64;
MNFSFSRSDF PEGFLFGTAT SAYQIEGHAF GGAGETHWDS FAATPGNVAK AENGARACDH
YHRWEEDLDL VAGGNFDVYR FSTSWARVMP DGVNVNPEGL DFYDRLVDGL LERGLKPAAT
LYHWELPSAL ADLGGWRNRD VAAWFGDFTA AIMGRIGDRV WSAAPINEPW CVSWLSHFLG
AHAPGLRDIR ATARAMHHVM LAHGTATQVM RDLGMSNLGA VCNLEYAQPA DQSPEAARVA
RIYDAIYNRF FLSGIFKGEY PAEVIEGLGD HLPEGWQDDM ALISQPVDWC GLNYYTRKLI
APAPGPWPGL AEVDGPLPKT EMGWEIYPEG LHHFLTMVAR DFTGTTPLHV TENGMAAPDR
LADGSVQDAD RIAYIDAHVT ALRRALAEGV PVSGYYVWSL MDNFEWALGY DKRFGLVHVD
FDSLERTPKA SYHALAQALS KD
//