BGLA_ASPFU
ID BGLA_ASPFU Reviewed; 873 AA.
AC Q4WJJ3;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=AFUA_1G05770;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000007; EAL88289.1; -; Genomic_DNA.
DR RefSeq; XP_750327.1; XM_745234.1.
DR PDB; 5FJI; X-ray; 1.95 A; A/B=30-873.
DR PDBsum; 5FJI; -.
DR AlphaFoldDB; Q4WJJ3; -.
DR SMR; Q4WJJ3; -.
DR STRING; 746128.CADAFUBP00000604; -.
DR Allergome; 8995; Asp f Glucosidase.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; BGL3A_ASPFU; -.
DR EnsemblFungi; EAL88289; EAL88289; AFUA_1G05770.
DR GeneID; 3507586; -.
DR KEGG; afm:AFUA_1G05770; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR InParanoid; Q4WJJ3; -.
DR OMA; EAQGYGF; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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..873
FT /note="Probable beta-glucosidase A"
FT /id="PRO_0000394095"
FT REGION 731..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 176..192
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 338..354
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 497..506
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 508..516
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 541..549
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 553..563
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 568..572
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 589..597
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 638..641
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 645..650
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 668..677
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 729..733
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 736..739
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 742..744
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 748..751
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 769..772
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 774..784
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 795..799
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 809..813
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 823..831
FT /evidence="ECO:0007829|PDB:5FJI"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:5FJI"
FT TURN 840..843
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 853..861
FT /evidence="ECO:0007829|PDB:5FJI"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:5FJI"
SQ SEQUENCE 873 AA; 94753 MW; F942110284B04E9F CRC64;
MRFGWLEVAA LTAASVANAQ VFDNSHGNNQ ELAFSPPFYP SPWADGQGEW ADAHRRAVEI
VSQMTLAEKV NLTTGTGWEM DRCVGQTGSV PRLGINWGLC GQDSPLGIRF SDLNSAFPAG
TNVAATWDKT LAYLRGKAMG EEFNDKGVDI LLGPAAGPLG KYPDGGRIWE GFSPDPALTG
VLFAETIKGI QDAGVIATAK HYILNEQEHF RQVGEAQGYG YNITETISSN VDDKTMHELY
LWPFADAVRA GVGAVMCSYN QINNSYGCQN SQTLNKLLKA ELGFQGFVMS DWSAHHSGVG
AALAGLDMSM PGDISFDDGL SFWGTNLTVS VLNGTVPAWR VDDMAVRIMT AYYKVGRDRL
RIPPNFSSWT RDEYGWEHSA VSEGAWTKVN DFVNVQRSHS QIIREIGAAS TVLLKNTGAL
PLTGKEVKVG VLGEDAGSNP WGANGCPDRG CDNGTLAMAW GSGTANFPYL VTPEQAIQRE
VISNGGNVFA VTDNGALSQM ADVASQSSVS LVFVNADSGE GFISVDGNEG DRKNLTLWKN
GEAVIDTVVS HCNNTIVVIH SVGPVLIDRW YDNPNVTAII WAGLPGQESG NSLVDVLYGR
VNPSAKTPFT WGKTRESYGA PLLTEPNNGN GAPQDDFNEG VFIDYRHFDK RNETPIYEFG
HGLSYTTFGY SHLRVQALNS SSSAYVPTSG ETKPAPTYGE IGSAADYLYP EGLKRITKFI
YPWLNSTDLE DSSDDPNYGW QDSEYIPEGA RDGSPQPLLK AGGAPGGNPT LYQDLVRVSA
TITNTGNVAG YEVPQLYVSL GGPNEPRVVL RKFDRIFLAP GEQKVWTTTL NRRDLANWDV
EAQDWVITKY PKKVHVGSSS RKLPLRAPLP RVY
