ID U5SA66_9LACT Unreviewed; 721 AA.
AC U5SA66;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=Q783_07945 {ECO:0000313|EMBL:AGY82120.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY82120.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY82120.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY82120.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006812; AGY82120.1; -; Genomic_DNA.
DR RefSeq; WP_023178674.1; NC_022606.1.
DR AlphaFoldDB; U5SA66; -.
DR STRING; 1266845.Q783_07945; -.
DR KEGG; caw:Q783_07945; -.
DR PATRIC; fig|1266845.5.peg.1482; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_9; -.
DR Proteomes; UP000017469; Chromosome.
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; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGY82120.1}.
FT DOMAIN 638..707
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 721 AA; 80089 MW; A3DC0FF91E29381D CRC64;
MDTTQLKHLL GEMTRAEKIG QMVQLAGEFY KEEDSENTGP MHEMNMTPKK MTVSGSVLGI
SGAETLINIQ KEHLAKSRLG IPLLFMADVV HGYRTIFPVP LAMASTWQPE LVEESANVSA
TEAAVSGLHV TFAPMVDLVR DARWGRVMES TGEDPYLNQL YARAFVRGYQ GQDLKNDPFS
VAACVKHFAG YGAPVAGREY NTVELSERTL KEMYLPAYQA GISEGSKLVM TAFNSLEGVP
ATANKPLMRE TLRKELGFEG VLISDWASVG ELIPHGIAKD LKQAGELAIQ AGVDIEMMTG
GYLNYLNELI DEGKVSEELL NEAVWRILTL KNELGLFENP YRGANSELEN NLVFSKEHRE
KARIVAEESI VLLKNEKQVL PLTHHQKVAL IVPKDQSKDV LGPWSWKGEP SESVSVYEGL
LNHISKEAIV VKTIDHSKND RPKDWLDDVS TADVIVAALG ESSYMSGEGA SRSNIKLPAE
QIQVIKELRT LNKPIVLILF NGRPLDLTDV VQDVDSILGA WFPGTEAGTA IGNILYGTKN
PSGKLTMSFP RAVGQVPLYY NQDNTGRPLT AYNQEDKYLS RYLDVDNRPL FPFGYGLSYT
QFSYSPMKVT LSKSEREQTD KIIVETTITN SGKVTGSEVV QLYIRDKVGQ VVRPIKELKR
FKKILLEPGE VATILFELNQ QDLEYVHQDL SVSVESGEFD LMIGSNSEEV ETTTVYLELK
K
//