Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable beta-glucosidase A

Gene

bglA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).By similarity

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei291By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.
mycoCLAPiBGL3A_ASPFU.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-glucosidase A (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase A
Cellobiase A
Gentiobiase A
Gene namesi
Name:bglA
Synonyms:bgl1
ORF Names:AFUA_1G05770
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiFungiDB:Afu1g05770.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei8995. Asp f Glucosidase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039409520 – 873Probable beta-glucosidase AAdd BLAST854

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi71N-linked (GlcNAc...)Sequence analysis1
Glycosylationi222N-linked (GlcNAc...)Sequence analysis1
Glycosylationi263N-linked (GlcNAc...)Sequence analysis1
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1
Glycosylationi333N-linked (GlcNAc...)Sequence analysis1
Glycosylationi365N-linked (GlcNAc...)Sequence analysis1
Glycosylationi453N-linked (GlcNAc...)Sequence analysis1
Glycosylationi534N-linked (GlcNAc...)Sequence analysis1
Glycosylationi553N-linked (GlcNAc...)Sequence analysis1
Glycosylationi575N-linked (GlcNAc...)Sequence analysis1
Glycosylationi679N-linked (GlcNAc...)Sequence analysis1
Glycosylationi725N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1873
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi48 – 50Combined sources3
Helixi51 – 61Combined sources11
Helixi66 – 73Combined sources8
Beta strandi80 – 87Combined sources8
Helixi91 – 93Combined sources3
Beta strandi100 – 102Combined sources3
Helixi120 – 126Combined sources7
Helixi129 – 145Combined sources17
Beta strandi149 – 151Combined sources3
Helixi168 – 170Combined sources3
Helixi176 – 192Combined sources17
Beta strandi196 – 203Combined sources8
Helixi213 – 218Combined sources6
Beta strandi228 – 230Combined sources3
Helixi233 – 238Combined sources6
Helixi242 – 249Combined sources8
Beta strandi253 – 257Combined sources5
Beta strandi259 – 262Combined sources4
Helixi267 – 269Combined sources3
Helixi271 – 274Combined sources4
Helixi275 – 281Combined sources7
Beta strandi286 – 290Combined sources5
Helixi299 – 304Combined sources6
Beta strandi308 – 315Combined sources8
Helixi325 – 332Combined sources8
Helixi338 – 354Combined sources17
Helixi357 – 360Combined sources4
Beta strandi372 – 378Combined sources7
Turni379 – 382Combined sources4
Beta strandi383 – 388Combined sources6
Turni397 – 399Combined sources3
Helixi400 – 409Combined sources10
Beta strandi412 – 418Combined sources7
Beta strandi427 – 433Combined sources7
Helixi434 – 436Combined sources3
Helixi447 – 449Combined sources3
Beta strandi460 – 463Combined sources4
Helixi473 – 483Combined sources11
Beta strandi487 – 491Combined sources5
Helixi497 – 506Combined sources10
Beta strandi508 – 516Combined sources9
Beta strandi528 – 531Combined sources4
Helixi541 – 549Combined sources9
Beta strandi553 – 563Combined sources11
Turni568 – 572Combined sources5
Beta strandi576 – 581Combined sources6
Helixi586 – 588Combined sources3
Helixi589 – 597Combined sources9
Beta strandi613 – 615Combined sources3
Helixi616 – 618Combined sources3
Beta strandi634 – 636Combined sources3
Turni638 – 641Combined sources4
Helixi645 – 650Combined sources6
Beta strandi668 – 677Combined sources10
Helixi704 – 707Combined sources4
Beta strandi724 – 727Combined sources4
Helixi729 – 733Combined sources5
Turni736 – 739Combined sources4
Helixi742 – 744Combined sources3
Turni748 – 751Combined sources4
Helixi769 – 772Combined sources4
Beta strandi774 – 784Combined sources11
Beta strandi786 – 788Combined sources3
Beta strandi790 – 792Combined sources3
Beta strandi795 – 799Combined sources5
Beta strandi809 – 813Combined sources5
Beta strandi816 – 818Combined sources3
Beta strandi823 – 831Combined sources9
Helixi832 – 835Combined sources4
Beta strandi837 – 839Combined sources3
Turni840 – 843Combined sources4
Beta strandi844 – 846Combined sources3
Beta strandi853 – 861Combined sources9
Beta strandi865 – 868Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FJIX-ray1.95A/B30-873[»]
ProteinModelPortaliQ4WJJ3.
SMRiQ4WJJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031215.
InParanoidiQ4WJJ3.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG092C0ZJY.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 4 hits.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4WJJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFGWLEVAA LTAASVANAQ VFDNSHGNNQ ELAFSPPFYP SPWADGQGEW
60 70 80 90 100
ADAHRRAVEI VSQMTLAEKV NLTTGTGWEM DRCVGQTGSV PRLGINWGLC
110 120 130 140 150
GQDSPLGIRF SDLNSAFPAG TNVAATWDKT LAYLRGKAMG EEFNDKGVDI
160 170 180 190 200
LLGPAAGPLG KYPDGGRIWE GFSPDPALTG VLFAETIKGI QDAGVIATAK
210 220 230 240 250
HYILNEQEHF RQVGEAQGYG YNITETISSN VDDKTMHELY LWPFADAVRA
260 270 280 290 300
GVGAVMCSYN QINNSYGCQN SQTLNKLLKA ELGFQGFVMS DWSAHHSGVG
310 320 330 340 350
AALAGLDMSM PGDISFDDGL SFWGTNLTVS VLNGTVPAWR VDDMAVRIMT
360 370 380 390 400
AYYKVGRDRL RIPPNFSSWT RDEYGWEHSA VSEGAWTKVN DFVNVQRSHS
410 420 430 440 450
QIIREIGAAS TVLLKNTGAL PLTGKEVKVG VLGEDAGSNP WGANGCPDRG
460 470 480 490 500
CDNGTLAMAW GSGTANFPYL VTPEQAIQRE VISNGGNVFA VTDNGALSQM
510 520 530 540 550
ADVASQSSVS LVFVNADSGE GFISVDGNEG DRKNLTLWKN GEAVIDTVVS
560 570 580 590 600
HCNNTIVVIH SVGPVLIDRW YDNPNVTAII WAGLPGQESG NSLVDVLYGR
610 620 630 640 650
VNPSAKTPFT WGKTRESYGA PLLTEPNNGN GAPQDDFNEG VFIDYRHFDK
660 670 680 690 700
RNETPIYEFG HGLSYTTFGY SHLRVQALNS SSSAYVPTSG ETKPAPTYGE
710 720 730 740 750
IGSAADYLYP EGLKRITKFI YPWLNSTDLE DSSDDPNYGW QDSEYIPEGA
760 770 780 790 800
RDGSPQPLLK AGGAPGGNPT LYQDLVRVSA TITNTGNVAG YEVPQLYVSL
810 820 830 840 850
GGPNEPRVVL RKFDRIFLAP GEQKVWTTTL NRRDLANWDV EAQDWVITKY
860 870
PKKVHVGSSS RKLPLRAPLP RVY
Length:873
Mass (Da):94,753
Last modified:July 5, 2005 - v1
Checksum:iF942110284B04E9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000007 Genomic DNA. Translation: EAL88289.1.
RefSeqiXP_750327.1. XM_745234.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00008981; CADAFUAP00008981; CADAFUAG00008981.
GeneIDi3507586.
KEGGiafm:AFUA_1G05770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000007 Genomic DNA. Translation: EAL88289.1.
RefSeqiXP_750327.1. XM_745234.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FJIX-ray1.95A/B30-873[»]
ProteinModelPortaliQ4WJJ3.
SMRiQ4WJJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei8995. Asp f Glucosidase.
CAZyiGH3. Glycoside Hydrolase Family 3.
mycoCLAPiBGL3A_ASPFU.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00008981; CADAFUAP00008981; CADAFUAG00008981.
GeneIDi3507586.
KEGGiafm:AFUA_1G05770.

Organism-specific databases

EuPathDBiFungiDB:Afu1g05770.

Phylogenomic databases

HOGENOMiHOG000031215.
InParanoidiQ4WJJ3.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG092C0ZJY.

Enzyme and pathway databases

UniPathwayiUPA00696.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 4 hits.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBGLA_ASPFU
AccessioniPrimary (citable) accession number: Q4WJJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: July 5, 2005
Last modified: November 2, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.