ID   BGL1B_PHACH             Reviewed;         540 AA.
AC   Q25BW4;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Beta-glucosidase 1B {ECO:0000303|PubMed:16896601, ECO:0000312|EMBL:BAE87009.1};
DE            EC=3.2.1.21;
DE   AltName: Full=Cellobiase 1B {ECO:0000303|PubMed:16896601};
GN   Name=BGL1B {ECO:0000312|EMBL:BAE87009.1};
OS   Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerodontia.
OX   NCBI_TaxID=2822231;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAE87009.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=K-3 {ECO:0000312|EMBL:BAE87009.1};
RC   TISSUE=Mycelium {ECO:0000269|PubMed:16896601};
RX   PubMed=16896601; DOI=10.1007/s00253-006-0526-z;
RA   Tsukada T., Igarashi K., Yoshida M., Samejima M.;
RT   "Molecular cloning and characterization of two intracellular beta-
RT   glucosidases belonging to glycoside hydrolase family 1 from the
RT   basidiomycete Phanerochaete chrysosporium.";
RL   Appl. Microbiol. Biotechnol. 73:807-814(2006).
RN   [2] {ECO:0000305}
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K-3 {ECO:0000269|PubMed:18023045};
RC   TISSUE=Mycelium {ECO:0000269|PubMed:18023045};
RX   PubMed=18023045; DOI=10.1002/bit.21717;
RA   Tsukada T., Igarashi K., Fushinobu S., Samejima M.;
RT   "Role of subsite +1 residues in pH dependence and catalytic activity of the
RT   glycoside hydrolase family 1 beta-glucosidase BGL1A from the basidiomycete
RT   Phanerochaete chrysosporium.";
RL   Biotechnol. Bioeng. 99:1295-1302(2008).
CC   -!- FUNCTION: Plays an important role in cellulose degradation. Shows
CC       hydrolytic activity against several glycosidic compounds.
CC       {ECO:0000269|PubMed:16896601}.
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:16896601};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.218 mM for cellobiose {ECO:0000269|PubMed:16896601,
CC         ECO:0000269|PubMed:18023045};
CC         KM=0.619 mM for p-nitrophenyl-beta-D-glucoside (pNP-Glu)
CC         {ECO:0000269|PubMed:16896601, ECO:0000269|PubMed:18023045};
CC         KM=4.02 mM for p-nitrophenyl-beta-D-galactoside (pNP-Gal)
CC         {ECO:0000269|PubMed:16896601, ECO:0000269|PubMed:18023045};
CC         KM=1.07 mM for cellobionolactone {ECO:0000269|PubMed:16896601,
CC         ECO:0000269|PubMed:18023045};
CC       pH dependence:
CC         Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:16896601,
CC         ECO:0000269|PubMed:18023045};
CC   -!- INDUCTION: Expressed in cellobiose culture, but repressed in glucose
CC       culture. {ECO:0000269|PubMed:16896601}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000255}.
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DR   EMBL; AB253327; BAE87009.1; -; mRNA.
DR   AlphaFoldDB; Q25BW4; -.
DR   SMR; Q25BW4; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   CLAE; BGL1B_PHACH; -.
DR   VEuPathDB; FungiDB:AGR57_4949; -.
DR   BRENDA; 3.2.1.21; 1380.
DR   SABIO-RK; Q25BW4; -.
DR   GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..540
FT                   /note="Beta-glucosidase 1B"
FT                   /id="PRO_0000390788"
FT   REGION          481..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT   ACT_SITE        380
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q25BW5,
FT                   ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT   BINDING         430
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT   BINDING         437..438
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  60665 MW;  D0B4518C9A11C071 CRC64;
     MSASAAPPNK LPADFLWGFA TASFQIEGAT DVDGRGKSIW DDFSKIPGKT LDGKNGDVAT
     DSYNRWREDV DLLVQYGVKS YRFSISWSRI IPLGGRNDPV NEAGIKFYSD LIDALLERGI
     VPFVTLYHWD LPQALHDRYL GWLNKDEIVQ DYVRYAGVCF ERFGDRVKHW LTMNEPWCIS
     ILGYGRGVFA PGRSSDRMRS PEGDSSTEPW IVGHSVILAH AYAVKLYREQ FKANRGGQIG
     ITLNGDWAMP YDDSPQNIEA AQHALDVAIG WFADPIYLGQ YPAYMKEMLG DRLPEFTPEE
     LAVVKGSSDF YGMNTYTTNL CKAGGEDEFQ GNVEYTFTRP DGTQLGTAAH CSWLQDYAPG
     FRDLLNYLYK RYRKPIYVTE NGFAVKDENS KPLEEALKDD DRVHYYQGVT DSLLAAVKED
     GVDVRGYFGW SLLDNFEWAD GYITRFGVTY VDYDTQKRYP KDSGKFLSQW FPAHIAESPK
     PAAETKKAAT PSPLKPHGAI SNGVSKKSSA TKEPKSASRK KGRKAPFARF TAYISAFLGL
//