ID A0A345QHG8_9RHOB Unreviewed; 437 AA.
AC A0A345QHG8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=C1J03_01130 {ECO:0000313|EMBL:AXI44755.1};
OS Sulfitobacter sp. SK012.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389005 {ECO:0000313|EMBL:AXI44755.1, ECO:0000313|Proteomes:UP000253903};
RN [1] {ECO:0000313|EMBL:AXI44755.1, ECO:0000313|Proteomes:UP000253903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK012 {ECO:0000313|EMBL:AXI44755.1,
RC ECO:0000313|Proteomes:UP000253903};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) 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; CP025804; AXI44755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345QHG8; -.
DR KEGG; sulz:C1J03_01130; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000253903; 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; 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:UP000253903}.
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 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 394
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 401..402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 437 AA; 48860 MW; FC6575828274F12B CRC64;
MKYKRSDFPE GFQFAAATSS YQIEGHGFGG AGLTHWDSFA ATPGNVVRGE HGQTACDHYH
RMEEDLDLCQ ALGLDAYRFS TSWARVLPEG RGQVNQEGLD FYDRLVDGCL ARGLNPMCTL
YHWELPAALA DEGGWRNADI GNWFADFTET IMSRIGDRVF SVAPINEPWC VSWLSHFEGH
HAPGLRDIRA TARAMHHVLV AHGRAIEVMR GLGVKNLGAV LNFEYAFAGD DTPEARQSAE
RYDAIYNQFF LGGIFNKSYP PLVLEGLEEH LPANWEKDFD TIAAPLDWVG VNYYTCKRIV
PADTGWPSLT DVPGPLQKTQ MDWEVYPEGL HHFLNLVHQA NGKNLPIYVT ESGMAQAVEP
GAADIQRTDY IDAHLGQTLR AIDEGLPVKG FTYWSVFDNY EWALGYEKRF GLVHVDFDTL
ERAPKASYHA LAAALAK
//
