ID A0A075P142_9ALTE Unreviewed; 446 AA.
AC A0A075P142;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=EP13_19070 {ECO:0000313|EMBL:AIG00615.1};
OS Alteromonas australica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=589873 {ECO:0000313|EMBL:AIG00615.1, ECO:0000313|Proteomes:UP000056090};
RN [1] {ECO:0000313|EMBL:AIG00615.1, ECO:0000313|Proteomes:UP000056090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 17 {ECO:0000313|EMBL:AIG00615.1,
RC ECO:0000313|Proteomes:UP000056090};
RA Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT "Genomes of Alteromonas australica, a world apart.";
RL Submitted (JUN-2014) 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|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; CP008849; AIG00615.1; -; Genomic_DNA.
DR RefSeq; WP_044058584.1; NZ_CP008849.1.
DR AlphaFoldDB; A0A075P142; -.
DR GeneID; 78256982; -.
DR KEGG; aal:EP13_19070; -.
DR eggNOG; COG2723; Bacteria.
DR Proteomes; UP000056090; Chromosome.
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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000056090}.
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 408..409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 446 AA; 50791 MW; 41268E3335A6FC4C CRC64;
MTKKLSLSST SPMMQPSFLF GTATSSFQIE GDAEGRLECI WDVFCRQAGA IADKSDGLRA
CEHVERWEED VNLIHSLGVD AYRLSISWPR VMHANGEINE QGLAFYKQLI DKLNSLNIKA
FVTLYHWDLP QYLEQRGGWL NRQTAYEFEN YVDKISAALG ERVYSYATFN EPFCSAYLGY
EIGVHAPGKT GREHGRTAAH HILLAHGLGM KMLKKNVPNA KNGIVLNFTP CYSASDSPAD
IAATEKADQY INQWYMQPVM EGCYPDVIHE LAEKDKPPIQ DGDMETICQP LDFLGINFYT
RLHYSAPRNH DELYFEHPHY EPKTDIGWEI HPPALTHLLT SLHQRYALPP VYITENGAAM
ADEVVDGRVE DNDRIEYYQN HLLAVEKAMD EGVKVSGYFA WSLMDNFEWA EGYEKRFGIV
YVDFDTQSRI LKDSAKAFKA LLAQRT
//
