BGL1A_PHACH
ID BGL1A_PHACH Reviewed; 462 AA.
AC Q25BW5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Beta-glucosidase 1A {ECO:0000303|PubMed:16896601, ECO:0000312|EMBL:BAE87008.1};
DE EC=3.2.1.21;
DE AltName: Full=Cellobiase 1A {ECO:0000303|PubMed:16896601};
GN Name=BGL1A {ECO:0000312|EMBL:BAE87008.1};
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:BAE87008.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=K-3 {ECO:0000312|EMBL:BAE87008.1};
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, AND MUTAGENESIS OF VAL-173; MET-177;
RP ASP-229; HIS-231 AND LYS-253.
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).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RC STRAIN=K-3 {ECO:0000269|PubMed:17376440};
RC TISSUE=Mycelium {ECO:0000269|PubMed:17376440};
RX PubMed=17376440; DOI=10.1016/j.febslet.2007.03.009;
RA Nijikken Y., Tsukada T., Igarashi K., Samejima M., Wakagi T., Shoun H.,
RA Fushinobu S.;
RT "Crystal structure of intracellular family 1 beta-glucosidase BGL1A from
RT the basidiomycete Phanerochaete chrysosporium.";
RL FEBS Lett. 581:1514-1520(2007).
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=6.80 mM for cellobiose {ECO:0000269|PubMed:16896601,
CC ECO:0000269|PubMed:18023045};
CC KM=0.229 mM for p-nitrophenyl-beta-D-glucoside (pNP-Glu)
CC {ECO:0000269|PubMed:16896601, ECO:0000269|PubMed:18023045};
CC KM=10.2 mM for p-nitrophenyl-beta-D-galactoside (pNP-Gal)
CC {ECO:0000269|PubMed:16896601, ECO:0000269|PubMed:18023045};
CC KM=0.752 mM for p-nitrophenyl-beta-D-xyloside (pNP-Xyl)
CC {ECO:0000269|PubMed:16896601, 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 constitutively in cellobiose and glucose cultures.
CC {ECO:0000269|PubMed:16896601}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000255}.
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DR EMBL; AB253326; BAE87008.1; -; mRNA.
DR PDB; 2E3Z; X-ray; 1.50 A; A/B=1-462.
DR PDB; 2E40; X-ray; 1.90 A; A/B=1-462.
DR PDBsum; 2E3Z; -.
DR PDBsum; 2E40; -.
DR AlphaFoldDB; Q25BW5; -.
DR SMR; Q25BW5; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR CLAE; BGL1A_PHACH; -.
DR VEuPathDB; FungiDB:AGR57_5510; -.
DR BRENDA; 3.2.1.21; 1380.
DR SABIO-RK; Q25BW5; -.
DR EvolutionaryTrace; Q25BW5; -.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
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; 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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation.
FT CHAIN 1..462
FT /note="Beta-glucosidase 1A"
FT /id="PRO_0000390787"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:17376440"
FT ACT_SITE 365
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17376440"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17376440"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17376440"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17376440"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17376440"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17376440"
FT BINDING 422..423
FT /ligand="substrate"
FT MUTAGEN 173
FT /note="V->C: 2-fold decrease in affinity for cellobiose."
FT /evidence="ECO:0000269|PubMed:18023045"
FT MUTAGEN 177
FT /note="M->L: Small decrease in affinity for cellobiose."
FT /evidence="ECO:0000269|PubMed:18023045"
FT MUTAGEN 229
FT /note="D->N: 17-fold decrease in affinity for cellobiose
FT and displays more acidic optimum pH than wild-type. No
FT effect on optimum pH; when associated with A-253."
FT /evidence="ECO:0000269|PubMed:18023045"
FT MUTAGEN 231
FT /note="H->D: 3-fold decrease in affinity for cellobiose."
FT /evidence="ECO:0000269|PubMed:18023045"
FT MUTAGEN 253
FT /note="K->A: 7-fold decrease in affinity for cellobiose. No
FT effect on optimum pH; when associated with N-229."
FT /evidence="ECO:0000269|PubMed:18023045"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2E3Z"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 140..158
FT /evidence="ECO:0007829|PDB:2E3Z"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 193..215
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 385..403
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:2E3Z"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:2E3Z"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2E3Z"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:2E3Z"
SQ SEQUENCE 462 AA; 52599 MW; 25C864094A8F5007 CRC64;
MSAAKLPKSF VWGYATAAYQ IEGSPDKDGR EPSIWDTFCK APGKIADGSS GDVATDSYNR
WREDVQLLKS YGVKAYRFSL SWSRIIPKGG RSDPVNGAGI KHYRTLIEEL VKEGITPFVT
LYHWDLPQAL DDRYGGWLNK EEAIQDFTNY AKLCFESFGD LVQNWITFNE PWVISVMGYG
NGIFAPGHVS NTEPWIVSHH IILAHAHAVK LYRDEFKEKQ GGQIGITLDS HWLIPYDDTD
ASKEATLRAM EFKLGRFANP IYKGEYPPRI KKILGDRLPE FTPEEIELVK GSSDFFGLNT
YTTHLVQDGG SDELAGFVKT GHTRADGTQL GTQSDMGWLQ TYGPGFRWLL NYLWKAYDKP
VYVTENGFPV KGENDLPVEQ AVDDTDRQAY YRDYTEALLQ AVTEDGADVR GYFGWSLLDN
FEWAEGYKVR FGVTHVDYET QKRTPKKSAE FLSRWFKEHI EE
