ID A0A058ZJC5_9RHOB Unreviewed; 441 AA.
AC A0A058ZJC5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=ATO10_12964 {ECO:0000313|EMBL:KCV81315.1};
OS Actibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1461693 {ECO:0000313|EMBL:KCV81315.1, ECO:0000313|Proteomes:UP000024836};
RN [1] {ECO:0000313|EMBL:KCV81315.1, ECO:0000313|Proteomes:UP000024836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-Z10 {ECO:0000313|Proteomes:UP000024836};
RA Lai Q., Li G., Shao Z.;
RT "Shimia sp. 22II-S11-Z10 Genome Sequencing.";
RL Submitted (APR-2013) 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:KCV81315.1}.
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DR EMBL; AQQY01000009; KCV81315.1; -; Genomic_DNA.
DR RefSeq; WP_035252267.1; NZ_AQQY01000009.1.
DR AlphaFoldDB; A0A058ZJC5; -.
DR STRING; 1461693.ATO10_12964; -.
DR PATRIC; fig|1461693.3.peg.2628; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000024836; 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; 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:UP000024836}.
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 22
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 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 404..405
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 441 AA; 49646 MW; 074A8B2248DAE3CC CRC64;
MQFTRSDFPE GFQFGVATSA YQIEGHAFGG AGATHWDSFA ATPGNVVRAE NGARGCDHYH
LYEQDLDLVA DAGFDCYRFS TSWARVLPEG RGSVNQAGLD FYDRLTDAML ERGIKPCATL
YHWELPSPLA DLGGWRNRDI AGWFADFTQI IMGRIGDRMH SVAPINEPWC VSWLSHFLGQ
HAPGLRDIRA TARAMHHVLL SHGRAIEVMR GLGMSNLGAV FNMEWADPAD DSDQARRAAD
VYDAYYNRFF IEGVFKKTYP DLVVEGLGPH LPWGWEDDFE TISTPVDWCG INYYTRKLMA
PNDGPWPHHH DVPGPLDKTQ MGWEIYPEGL YKFLTRTARE YSGQMPIIVT ENGMANEDAL
INGAVNDQRR IAYINSHIDA AQRAMAEGVP LNGYFLWSLL DNYEWALGYE KRFGLVHVDF
ETMKRTPKAS YLSLSQALNA G
//