BGLA_ASPOR
ID BGLA_ASPOR Reviewed; 861 AA.
AC Q2UUD6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable beta-glucosidase A;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase A;
DE AltName: Full=Cellobiase A;
DE AltName: Full=Gentiobiase A;
DE Flags: Precursor;
GN Name=bglA; Synonyms=bgl1; ORFNames=AO090009000356;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose (By similarity).
CC {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AP007150; BAE54829.1; -; Genomic_DNA.
DR RefSeq; XP_001816831.1; XM_001816779.2.
DR PDB; 5FJJ; X-ray; 1.95 A; A/B/C/D=20-861.
DR PDBsum; 5FJJ; -.
DR AlphaFoldDB; Q2UUD6; -.
DR SMR; Q2UUD6; -.
DR STRING; 510516.Q2UUD6; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; BAE54829; BAE54829; AO090009000356.
DR GeneID; 5988761; -.
DR KEGG; aor:AO090009000356; -.
DR VEuPathDB; FungiDB:AO090009000356; -.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; EAQGYGF; -.
DR BRENDA; 3.2.1.21; 522.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006564; Chromosome 1.
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:0016052; P:carbohydrate catabolic process; IDA:AspGD.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR026891; Fn3-like.
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 InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..861
FT /note="Probable beta-glucosidase A"
FT /id="PRO_0000394097"
FT REGION 730..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 166..182
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 463..472
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 487..496
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 498..506
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 531..541
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 543..553
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 558..562
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 566..571
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 579..587
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 617..620
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 628..631
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 635..640
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 658..667
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 692..695
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 717..721
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 724..727
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 736..739
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 757..760
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 762..772
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 797..801
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 811..819
FT /evidence="ECO:0007829|PDB:5FJJ"
FT HELIX 820..823
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:5FJJ"
FT TURN 828..831
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 841..849
FT /evidence="ECO:0007829|PDB:5FJJ"
FT STRAND 853..856
FT /evidence="ECO:0007829|PDB:5FJJ"
SQ SEQUENCE 861 AA; 93415 MW; 867B9B1DC8301DDA CRC64;
MKLGWIEVAA LAAASVVSAK DDLAYSPPFY PSPWADGQGE WAEVYKRAVD IVSQMTLTEK
VNLTTGTGWQ LERCVGQTGS VPRLNIPSLC LQDSPLGIRF SDYNSAFPAG VNVAATWDKT
LAYLRGQAMG EEFSDKGIDV QLGPAAGPLG AHPDGGRNWE GFSPDPALTG VLFAETIKGI
QDAGVIATAK HYIMNEQEHF RQQPEAAGYG FNVSDSLSSN VDDKTMHELY LWPFADAVRA
GVGAVMCSYN QINNSYGCEN SETLNKLLKA ELGFQGFVMS DWTAHHSGVG AALAGLDMSM
PGDVTFDSGT SFWGANLTVG VLNGTIPQWR VDDMAVRIMA AYYKVGRDTK YTPPNFSSWT
RDEYGFAHNH VSEGAYERVN EFVDVQRDHA DLIRRIGAQS TVLLKNKGAL PLSRKEKLVA
LLGEDAGSNS WGANGCDDRG CDNGTLAMAW GSGTANFPYL VTPEQAIQNE VLQGRGNVFA
VTDSWALDKI AAAARQASVS LVFVNSDSGE GYLSVDGNEG DRNNITLWKN GDNVVKTAAN
NCNNTVVIIH SVGPVLIDEW YDHPNVTGIL WAGLPGQESG NSIADVLYGR VNPGAKSPFT
WGKTRESYGS PLVKDANNGN GAPQSDFTQG VFIDYRHFDK FNETPIYEFG YGLSYTTFEL
SDLHVQPLNA SRYTPTSGMT EAAKNFGEIG DASEYVYPEG LERIHEFIYP WINSTDLKAS
SDDSNYGWED SKYIPEGATD GSAQPRLPAS GGAGGNPGLY EDLFRVSVKV KNTGNVAGDE
VPQLYVSLGG PNEPKVVLRK FERIHLAPSQ EAVWTTTLTR RDLANWDVSA QDWTVTPYPK
TIYVGNSSRK LPLQASLPKA Q
