ID J2S7D3_FLASC Unreviewed; 886 AA.
AC J2S7D3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=PMI10_03515 {ECO:0000313|EMBL:EJL61162.1};
OS Flavobacterium sp. (strain CF136).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1144313 {ECO:0000313|EMBL:EJL61162.1, ECO:0000313|Proteomes:UP000007287};
RN [1] {ECO:0000313|EMBL:EJL61162.1, ECO:0000313|Proteomes:UP000007287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF136 {ECO:0000313|EMBL:EJL61162.1,
RC ECO:0000313|Proteomes:UP000007287};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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 -!- 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:EJL61162.1}.
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DR EMBL; AKJZ01000061; EJL61162.1; -; Genomic_DNA.
DR RefSeq; WP_007810313.1; NZ_AKJZ01000061.1.
DR AlphaFoldDB; J2S7D3; -.
DR STRING; 1144313.PMI10_03515; -.
DR PATRIC; fig|1144313.4.peg.3498; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000007287; 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; 2.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
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 Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EJL61162.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..886
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003754194"
FT DOMAIN 493..631
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 886 AA; 98872 MW; E776852FC00F4199 CRC64;
MLQLRMKKTA IIFVMALGFF NQSSAQKKYP YQDAKMPVED RVKDLLSRMS LEEKVRQMDM
YKGEYFKDKE DFSKTKSDAK IGNLGIGAIH DIYPRSAKMI NDLQSEVIKK NKWGIPALIM
CEMLHGYLDD GSTAFPMSIG LGSTWDTSLM DKVGKVIGTE ARAHGVHFGL GPNLDVGLEP
RWGRVAETFG EDVYLNSEIG LAMIKGMQGE DLKSDRSIIA EPKHFAVHGI PQAGGNASPV
LVGERSARQD FLPSFEKAFR KGGALGTMCA YSELDGIPCA ANHWLLTDVL RKEWGFKGIV
VSDLGAIKYL QTTHYVTDSP KESIRTAISA GVDMQFYDFT NEFWQQTIID LVNEKKLTME
QIDRAAGGVL RLKFLLGLFE NPYTDKNLIK ERFHTKENQD IALEAGHKSI VLLKNENNIL
PLKKDIKTIA VIGPNANASR LGGYSVKNKV GTTVLEGIKQ VVGAKTNVLY EEGVPLIVMG
QVIPKAYLFT PDESQNGLKG EYFNNRNLEG TPALTRIDSQ LEFDWPWSPG DGVADDDFSI
RWTGFIKSEK AFDGWLGLSS DDGIRMWIDD QLVIDNWTKG ATNMVTTPKN IEAGKKYKVR
IEMWEGGWGA RAHLRWNLEK VNLQPAIDAA KKADVAIVVL GESNELVEEN RDVATLDLHG
MQQELIEAIQ KTGTPVVCVL LNGRPLSVNW ISENIPAIVE GWFPGEAGGK AVADVLFGDY
NPGGRLPVTF PKSVGQLPIY YNQKPSAIHR YVSESENPLY TFGYGLSYTK FEYSNFNLNT
KEIKPDGELK VSVDVKNTGN YDGDEVVQLY INDVYSSVTT PRKTLKGFKR LFIKKGETKQ
VEFVLTPEEL SLWNREMKRV VEPGDFEVMV GGNSVDLQKL SFRVVN
//
