BGLFU_BIFBR
ID BGLFU_BIFBR Reviewed; 460 AA.
AC P94248; O08487;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Bifunctional beta-D-glucosidase/beta-D-fucosidase;
DE EC=3.2.1.21;
DE EC=3.2.1.38;
OS Bifidobacterium breve.
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=1685;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA19881.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8988633; DOI=10.1271/bbb.60.2011;
RA Nunoura N., Ohdan K., Tanaka K., Tamaki H., Yano T., Inui M., Yukawa H.,
RA Yamamoto K., Kumagai H.;
RT "Cloning and nucleotide sequence of the beta-D-glucosidase gene from
RT Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in
RT Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 60:2011-2018(1996).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9063964; DOI=10.1271/bbb.60.188;
RA Nunoura N., Ohdan K., Yano T., Yamamoto K., Kumagai H.;
RT "Purification and characterization of beta-D-glucosidase (beta-D-
RT fucosidase) from Bifidobacterium breve clb acclimated to cellobiose.";
RL Biosci. Biotechnol. Biochem. 60:188-193(1996).
CC -!- FUNCTION: Bifunctional beta-D-glucosidase/beta-D-fucosidase. Activity
CC towards pNP-beta-D-fucoside is about 80-85% of the activity towards
CC pNP-beta-D-glucoside. Also has slight activity (less than 10%) towards
CC pNP-beta-D-galactoside, and very low activity (less than 1%) towards
CC pNP-beta-D-xyloside. Hydrolyzes laminaribiose, sophorose, cellobiose
CC and gentobiose. Not active against maltose, pNP-alpha-D-glucoside or
CC pNP-beta-L-fucoside. {ECO:0000269|PubMed:8988633,
CC ECO:0000269|PubMed:9063964}.
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:0000269|PubMed:8988633, ECO:0000269|PubMed:9063964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fucose residues in
CC beta-D-fucosides.; EC=3.2.1.38; Evidence={ECO:0000269|PubMed:8988633,
CC ECO:0000269|PubMed:9063964};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+), Ag(+) and Hg(+), but not by
CC other cations such as Mg(2+), Ca(2+), Mn(2+) and Co(2+). Inhibited by
CC 1-amino-1-deoxy-D-glucose and p-chloromercuribenzoic acid, but not by
CC EDTA or dithiothreitol. Inhibited by the disaccharides sucrose, lactose
CC and cellobiose. The monosaccharides D-fructose, D-mannose, D-xylose and
CC D-glucose increase the beta-D-fucosidase activity, but not the beta-D-
CC glucosidase activity. D-glucose inhibits the beta-D-glucosidase
CC activity, but promotes the beta-D-fucosidase activity. D-fucose
CC inhibits the beta-D-glucosidase activity and does not significantly
CC affect the beta-D-fucosidase activity. {ECO:0000269|PubMed:9063964}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for pNP-beta-D-glucoside {ECO:0000269|PubMed:8988633,
CC ECO:0000269|PubMed:9063964};
CC KM=0.7 mM for pNP-beta-D-fucoside {ECO:0000269|PubMed:8988633,
CC ECO:0000269|PubMed:9063964};
CC pH dependence:
CC Optimum pH is 5.5 with pNP-beta-D-glucoside as a substrate. Retains
CC more than 90% of its activity between pH 5.0 and 7.0. Retains 70% of
CC its activity at pH 4.5 and 8.5. {ECO:0000269|PubMed:8988633,
CC ECO:0000269|PubMed:9063964};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius with pNP-beta-D-glucoside
CC as a substrate. Retains 60% of its activity after 10 minutes
CC incubation at 50 degrees Celsius. {ECO:0000269|PubMed:8988633,
CC ECO:0000269|PubMed:9063964};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9063964}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9063964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000255}.
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DR EMBL; D88311; BAA19881.1; -; Genomic_DNA.
DR PIR; JC5137; JC5137.
DR AlphaFoldDB; P94248; -.
DR SMR; P94248; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR SABIO-RK; P94248; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IEA:UniProtKB-EC.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR03356; BGL; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9063964"
FT CHAIN 2..460
FT /note="Bifunctional beta-D-glucosidase/beta-D-fucosidase"
FT /evidence="ECO:0000269|PubMed:9063964"
FT /id="PRO_0000395428"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT ACT_SITE 362
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5,
FT ECO:0000255|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 460 AA; 51514 MW; 5FD80CB8AB6888A9 CRC64;
MTMIFPKGFM FGTATAAYQI EGAVAEGGRT PSIWDTFSHT GHTLNGDTGD VADDFYHRWE
DDLKLLRDLG VNAYRFSIGI PRVIPTPDGK PNQEGLDFYS RIVDRLLEYG IAPIVTLYHW
DLPQYMASGD GREGGWLERE TAYRIADYAG IVAKCLGDRV HTYTTLNEPW CSAHLSYGGT
EHAPGLGAGP LAFRAAHHLN LAHGLMCEAV RAEAGAKPGL SVTLNLQICR GDADAVHRVD
LIGNRVFLDP MLRGRYPDEL FSITKGICDW GFVCDGDLDL IHQPIDVLGL NYYSTNLVKM
SDRPQFPQST EASTAPGASD VDWLPTAGPH TEMGWNIDPD ALYETLVRLN DNYPGMPLVV
TENGMACPDK VEVGTDGVKM VHDNDRIDYL RRHLEAVYRA IEEGTDVRGY FAWSLMDNFE
WAFGYSKRFG LTYVDYESQE RVKKDSFDWY RRFIADHSAR
