BGL1B_PHACH
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 03-AUG-2022, entry version 59.
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}.
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; 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 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; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 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
