ID A0A5S5DL68_9SPHI Unreviewed; 759 AA.
AC A0A5S5DL68;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 8.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BC792_105163 {ECO:0000313|EMBL:TYP96670.1};
OS Sphingobacterium composti Yoo et al. 2007 non Ten et al. 2007.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=415956 {ECO:0000313|EMBL:TYP96670.1, ECO:0000313|Proteomes:UP000325105};
RN [1] {ECO:0000313|EMBL:TYP96670.1, ECO:0000313|Proteomes:UP000325105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18850 {ECO:0000313|EMBL:TYP96670.1,
RC ECO:0000313|Proteomes:UP000325105};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUL-2019) 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:TYP96670.1}.
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DR EMBL; VNHX01000005; TYP96670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5S5DL68; -.
DR OrthoDB; 9758670at2; -.
DR Proteomes; UP000325105; 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:SF121; PERIPLASMIC 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|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000325105};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..759
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024460962"
FT DOMAIN 679..748
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 759 AA; 83330 MW; F894914B9E5A3C69 CRC64;
MKKIAIWMLS FAATCSWSVK AQTDPKMETF ISGLMSKMTV EEKIGQLNLV TGGEAVTGSV
VSTGVETKIK AGQIGGIFSM SSPSKIRAAQ ELAVKHSRLG IPIIFGMDVI HGYKTMFPIP
LGLAATWDMD LIRETARIAA VEATADGLNW TFSPMVDISR DPRWGRISEG SGEDTYLSAR
IAAEMVKGYQ GSNLAANNTL MACVKHFALY GAAESGRDYN TTDMSLHRMY NEYLPPYKAA
IDAGAWTVMA SFNDINGVPA TANKWLLTDV LRKQWGFNGM VVTDYTGINE LVDHGLGDLQ
TVSALALKAG IHMDMVGEGF LTTLKKSLDE GKVSIEEIDE ACRLVLKAKY KLGLFDDPYR
YCDEERAKGN ILTPAHLAKA RETAAKSFVL LKNDKQTLPL KKNGTVALIG PLANTGPNMP
GTWSVSADLE NTPSLLEGMR AVLGGQVDIV HHLGANLMSD PHYQERATMF GRTIPRDERP
EEQIIAEALE VAKSADVIVA ALGESSEMSG ESSSRTDLGI PDTQRRLLEA LLQTGKPVVL
VLFTGRPLTL TWEHEHVPAI LNVWFGGTET GKAVADVLFG DVNPSGKLPA TFPQNVGQIP
LYYSAKNTGR PLAEGAWFQK FRSNYLDVNN QPLYPFGYGL SYSTFEYSDI RLDKNSITAD
EKILATVTVK NTGNYDGEEV VQLYLRDSYA SVTRPVKELK AFQKIFLKKG ESRDVSFEIG
IDDLKFYNNE LQWEAEPGDF VVFIGTNSRD LKEAKFTLR
//
