BGLA_ARTBC
ID BGLA_ARTBC Reviewed; 820 AA.
AC D4AN50;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Probable beta-glucosidase ARB_05654 {ECO:0000305};
DE EC=3.2.1.21 {ECO:0000250|UniProtKB:P87076};
DE AltName: Full=Allergen Asp n 14 homolog {ECO:0000305};
DE AltName: Full=Beta-D-glucoside glucohydrolase {ECO:0000250|UniProtKB:P87076};
DE Flags: Precursor;
GN ORFNames=ARB_05654;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass (By similarity).
CC Catalyzes the last step releasing glucose from the inhibitory
CC cellobiose (By similarity). {ECO:0000250|UniProtKB:P87076}.
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:0000250|UniProtKB:P87076};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000250|UniProtKB:P87076}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; ABSU01000003; EFE35611.1; -; Genomic_DNA.
DR RefSeq; XP_003016256.1; XM_003016210.1.
DR AlphaFoldDB; D4AN50; -.
DR SMR; D4AN50; -.
DR STRING; 663331.D4AN50; -.
DR EnsemblFungi; EFE35611; EFE35611; ARB_05654.
DR GeneID; 9524327; -.
DR KEGG; abe:ARB_05654; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; EAQGYGF; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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-UniPathway.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
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 Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 1: Evidence at protein level;
KW Allergen; Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..820
FT /note="Probable beta-glucosidase ARB_05654"
FT /id="PRO_0000434931"
FT ACT_SITE 304
FT /evidence="ECO:0000250|UniProtKB:P29090"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 820 AA; 88839 MW; FAF09AAF11363E9D CRC64;
MLFRWCPLVA LAIASGTAAT EQSWESSPYY PSPWTKGEGE WEAAYQKAVS FVSQLTLDEK
VNLTTGVGWM QESCVGQVGS IPRLGFRSLC MQDGPLGIRF GTEARMDIFL YLTCNTNFYL
PYVGDYVTAF PAGINVAATW SRELAYLRGK AMGEEFRGKG ADVILGPAIG PIGRAPEGGR
NWEGLGPDPV LAGKLVAETI KGMQKSGVIA CAKHFIANEQ ERFRIAAEAQ GYGFDIAESI
SSNVDDVTMH EIYLWPFADA VKAGVGSIMC SYNQINNSYG CGNSYTQNKL LKGELGFRGF
IMSDWQAHHS GVGSAFAGLD MSMPGDTLFG TGVSYWGANL TIAVANGTIP EWRVDDMAVR
IMAAYYKVGR DQVQVPINFN SWTTDVEGYQ HALVKEGYGV VNQRVNVRDH HAQIARRVAR
DSTVLLKNKG VLPLTGTEQF TAIIGEDAGP NINGPNSCPD RGCDNGTLAM GWGSGTTNFP
YLVTPDDAIQ REIVGKGVGN VMSVLQNGDF KNIQAVAGQA DVALVFINSD SGEGYISVDG
NEGDRKNLTT WKGGDEMVKQ VTSVCNNTVL VIHSSGPILA GQWHDNPNIT AILWAGLPGQ
ESGNALVDIL YGKENPGGKS PFTWGRAAED YGTTILREPN NGKGAPQHLF SEGIMFEYRH
FDQKNITPVY EFGYGLSYTT FSYSDLRVRP MRANKYVPAT GMTKPAPRLG HSSTKYADYL
FPGGFKGVTK YVYPWLTSTD PKEASGDKNY GMPLEDYVPP NANNGDAQPV LPASGVPGGN
PGLFEDLYEV SAVITNDGDR VGEEVPQLVR NLSFFPPILS
