ID A0A5P2G8R0_9BACT Unreviewed; 760 AA.
AC A0A5P2G8R0;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=bglX {ECO:0000313|EMBL:QES89603.1};
GN ORFNames=E0W69_013335 {ECO:0000313|EMBL:QES89603.1};
OS Arachidicoccus sp. B3-10.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=2545455 {ECO:0000313|EMBL:QES89603.1, ECO:0000313|Proteomes:UP000292424};
RN [1] {ECO:0000313|EMBL:QES89603.1, ECO:0000313|Proteomes:UP000292424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3-10 {ECO:0000313|EMBL:QES89603.1,
RC ECO:0000313|Proteomes:UP000292424};
RA Kim H.S., Han K.-I., Suh M.K., Lee K.C., Eom M.K., Kim J.-S., Kang S.W.,
RA Sin Y., Lee J.-S.;
RT "Complete genome sequence of Arachidicoccus sp. B3-10 isolated from apple
RT orchard soil.";
RL Submitted (SEP-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}.
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DR EMBL; CP044016; QES89603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5P2G8R0; -.
DR KEGG; arac:E0W69_013335; -.
DR OrthoDB; 721009at2; -.
DR Proteomes; UP000292424; 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: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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:QES89603.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000292424};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..760
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024336407"
FT DOMAIN 679..748
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 760 AA; 83094 MW; 469327E2F5470157 CRC64;
MRLKQWIVLS SIVGCVSSLN AQQNEMNKFV SNLMSKMTTD EKIGQLNQEA VSDGVLTGSI
VQGGVDEKIK KGQVGSTFGI WGASKLRRLQ EMAVNNSRLH IPLLFGLDVI HGHRTLFPIP
LGISTSWDLN LIQQSAHYAA KEATADGLKW VFSPMVDIAR DPRWGRVSEG SGEDPYLGSL
IAKAMIKGYQ GNSLADTMNV LACIKHFALY GGAEAGREYN TVDMSLIKMY EYYFPPYKAA
VDAGAASVMT SFNDLNGVPS TANRWLLTDV LRKQWGFNGL VVTDYTAVSE LIAHGIGKDL
QEVSAKSLAA GTDMDMVSEG FLNTLGKSLK EGKITIAQID SACKRVLEAK YKAGLFKNPY
AGLDSNRYEK EILTKENRAF ARKLASHSMV LLKNENQILP LQKKGTIALV GPLADSRRNM
LGTWSVSGEW DKAVTVKEGI ENAVDGKAKI IYAKGANISD DTLFNQKVNV FGEEISIDEK
SPETLIKEAV DAANNSDVVV AVVGEAADMT GESSSRSHID IPESQAKLLR ALVATGKPVV
AVLFNGRPLT LDWEKEHLTG ILDAWFGGTE GGNAIADILF GDYNPSGKLT MTFPRNVGQI
PIYYNHKNTG RPYVEGGPTK FKSDYLDVPN TPLYPFGYGL SYTTFAYDAP TISNTHPKGN
APVKLSVKVS NTGKYAGEET VQLYISDPVA SVTRSVEDLK GFQKVYLNPG ESKVVNFIID
TESLKFYNAN LKYDWEPGEF TFRVGTNSED TKAVTVHWDK
//
