GenomeNet

Database: UniProt
Entry: A0A099CYQ1_9GAMM
LinkDB: A0A099CYQ1_9GAMM
Original site: A0A099CYQ1_9GAMM 
ID   A0A099CYQ1_9GAMM        Unreviewed;       450 AA.
AC   A0A099CYQ1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=LF63_0100980 {ECO:0000313|EMBL:KGI79093.1};
OS   Oleiagrimonas soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Oleiagrimonas.
OX   NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI79093.1, ECO:0000313|Proteomes:UP000029708};
RN   [1] {ECO:0000313|EMBL:KGI79093.1, ECO:0000313|Proteomes:UP000029708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3.5X {ECO:0000313|EMBL:KGI79093.1,
RC   ECO:0000313|Proteomes:UP000029708};
RA   Fang T., Wang H.;
RT   "Xanthomonadaceae 3.5X direct submission.";
RL   Submitted (SEP-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}.
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:KGI79093.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JROI01000003; KGI79093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099CYQ1; -.
DR   STRING; 1543381.LF63_0100980; -.
DR   HOGENOM; CLU_001859_1_0_6; -.
DR   Proteomes; UP000029708; 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; LACTASE-LIKE PROTEIN; 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:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029708}.
FT   ACT_SITE        167
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         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         400
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         407..408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   450 AA;  51103 MW;  D8ED0FBCDBFFB6DB CRC64;
     MPENMRFPET FLWGCATSAY QIEGSPLADG AGPSIWERFA HTPGMMHNDD HGDIACDHYH
     RFRDDVKLMR DLGLTSYRFS IAWARILPAG TGAVNQKGLD FYRQLVDALR EGGITPMATL
     YHWDLPEALD DRGGWLNRDS ADWFAEYATT CFEALDDRVP LWVTLNEPWV VTDGGYLHGV
     LAPGHRSPYE TARVTHHLMR AHGAAVQAYR AVGKHQIGLV VNLEPKYPAS DRAEDRAATQ
     RADAYMNRQY LDPALKGSYP PEMRDIFGDA WRDWPAADLE QIRQPIDFLG VNYYTRGLTA
     HDATAWPLRA RTRRVPQATY TETDWEVYEQ GLTDILTWVK QRYGDIPLYV TENGAAFYDP
     PVAAADGVHD PLRIDYLRRH LRAVHKAIAQ GADVRGYYLW SLLDNLEWSL GFAKRFGIVH
     VNYETLQRTP KDSAKFYAEV IASHGESLSD
//
DBGET integrated database retrieval system