ID   Q1YTH0_9GAMM            Unreviewed;       771 AA.
AC   Q1YTH0;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=GB2207_01897 {ECO:0000313|EMBL:EAS47517.1};
OS   gamma proteobacterium HTCC2207.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS47517.1, ECO:0000313|Proteomes:UP000005555};
RN   [1] {ECO:0000313|EMBL:EAS47517.1, ECO:0000313|Proteomes:UP000005555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS47517.1,
RC   ECO:0000313|Proteomes:UP000005555};
RA   Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) 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|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EAS47517.1}.
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DR   EMBL; AAPI01000002; EAS47517.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YTH0; -.
DR   STRING; 314287.GB2207_01897; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000005555; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..771
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004197830"
FT   DOMAIN          688..757
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   771 AA;  84838 MW;  22894605DCC9EAD7 CRC64;
     MKKLLLSFTG LLISTVSLTS ISSELLPAYL DASLTPEQRV ADLLPRMTLE EKVGQMCQYV
     GIDHTAESEQ QMSIDDLAKS DAQGFYPDLH SSQIPAFIET GKVGSFLHVL TASEANLLQR
     HAAQSRLGIP LLIGIDAIHG NAMVSGSTVY PAPLSMASSW NLGLVKQASI ETAREMRATG
     SHWSFTPNVD IARDPRWGRV GETFGEDPFL VAEMGVATIE GLQQRDFDGP QKVIANAKHW
     VAGGDPINGI NLSPMDVSER SLRQDFFPPF KRAVDAGVFT FMAAHNEING EPAHGSRYLL
     NDVLREEWGF KGFVVSDWMD IERLHTFHRV ANSQKEAVYQ TVHAGMDMHM HGPDFLEPLV
     ELVNEGRLSE ARIDESVGPM LLAKFRLGLF ENPYVDESQI EQSVFTAAHQ QTALEMARQA
     IVLLTNNDNI LPLQKNSRVF VTGPNADNHT ILGDWVLEQP ENNVTTVLEG LRAVAASPKN
     IDFYDVGKQV KNLSTEDILA AAKRASQSQV AVVVVGENPL RYDKKGKTSG ENVARSSINL
     IGRQLELVQA IHATGTPVIV VLVNGRPIAE PWVVDNSAAV IEAWEPGAMG GQALAEIIYG
     VTNPSGKLPI TVPYSIGHTQ AIYNHKPSAY KHKYADAPTR NLFEFGYGLS YTEFAFSPPV
     LDKKSIQKTE NTNLSVTVTN SGDRAGYETV QLYVRDNYSE ITRPVKELKG FEKIYLQAGE
     SKRVSFTLEP EMLAYYNRAM EWVVEPGAFT LMVGSSSRGA DLKSIQLRVK D
//