ID A0A148KN72_9ALTE Unreviewed; 851 AA.
AC A0A148KN72;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AX660_19580 {ECO:0000313|EMBL:KXI27747.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI27747.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI27747.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI27747.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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}.
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:KXI27747.1}.
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DR EMBL; LSNE01000009; KXI27747.1; -; Genomic_DNA.
DR RefSeq; WP_068379185.1; NZ_LSNE01000009.1.
DR AlphaFoldDB; A0A148KN72; -.
DR STRING; 1799789.AX660_19580; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000070299; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
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 InterPro; IPR041443; Exop_C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF18559; Exop_C; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000070299};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..851
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007550188"
FT DOMAIN 71..395
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 436..650
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT DOMAIN 685..836
FT /note="ExoP galactose-binding-like"
FT /evidence="ECO:0000259|Pfam:PF18559"
SQ SEQUENCE 851 AA; 92555 MW; 9BABBF5A1E644D7B CRC64;
MKFSLSYFAI PAALFTLSAC SDNPAIPSSA KSSDNSQSAT QVPDFWPVLD IAIKTDAGVE
KQVAELLAKM TIEQKVAQTI QPEIRDITVE DMRQYGFGSF LNGGGAFPDN NKHATPQDWI
AVAQAMYLAS VDDSLDGSKI PTMWGTDAVH GHNNVIGATL FPHNIGLGAM HNPALIKEIA
KATAAEVMAT GIDWVFAPTV ATVQDDRWGR TYESYSEDPA IIRQYSQAIV EGLQGDPQSG
YFKDDNVIST VKHFVGDGGT VKGDDQGDNL STEQQLFELH AQGYVGGLSA GAQVVMASFN
SWHGEKLHGH QYLLTDVLKK RMGFDGFVVG DWNGHGQVLG CSNESCPQAM NAGLDVYMVA
TPAWKPLYEN TLAQVKSGEI PLARLDDAVT RILRVKVRAG LFTKPAPSER KYANLNNVIG
NDAHRAVARQ AVRESLVLLK NNGQLLPLKA TQAFLLAGDG ADNIGKQSGG WTITWQGTGN
NNDDFLGGHS IYDGIKSRVE AAGGSIELAV NGEYQQKPDV AIVVFGEEPY AEGNGDIDNL
EYQRGNKTDL ALLRKLSAQG IPTVAIFLSG RPLWVNPELN ASDAFIAAWL PGSEGQGVAD
VILADDSGKA EFDFIGRLPF SWPTTPTQTP LNFYDADYQP LFKLGYGLSY NSHAELSNEL
SEVVEKTEQN IQTKVLFERS AITPLYVAIN EDNQTLRMNS NSLMTPNIKV RTTDRTVQED
ALQITWLTDQ VSKFSLQSDF PDDLRSSLEA NSSLQFDIKL NSLSEPQIEL LIECGDACNG
RVVLKEQLEN QQSSWQTMSI DLGCFAQQGV DFSKIYSPFA LTANKDTQIE LSNIRLVANS
ADVATIQCAA N
//