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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei291 – 2911By similarity

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

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 873854Probable beta-glucosidase APRO_0000394095Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence analysis
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence analysis
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence analysis
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence analysis
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence analysis
Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence analysis
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence analysis
Glycosylationi575 – 5751N-linked (GlcNAc...)Sequence analysis
Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence analysis
Glycosylationi725 – 7251N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
873
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503Combined sources
Helixi51 – 6111Combined sources
Helixi66 – 738Combined sources
Beta strandi80 – 878Combined sources
Helixi91 – 933Combined sources
Beta strandi100 – 1023Combined sources
Helixi120 – 1267Combined sources
Helixi129 – 14517Combined sources
Beta strandi149 – 1513Combined sources
Helixi168 – 1703Combined sources
Helixi176 – 19217Combined sources
Beta strandi196 – 2038Combined sources
Helixi213 – 2186Combined sources
Beta strandi228 – 2303Combined sources
Helixi233 – 2386Combined sources
Helixi242 – 2498Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi259 – 2624Combined sources
Helixi267 – 2693Combined sources
Helixi271 – 2744Combined sources
Helixi275 – 2817Combined sources
Beta strandi286 – 2905Combined sources
Helixi299 – 3046Combined sources
Beta strandi308 – 3158Combined sources
Helixi325 – 3328Combined sources
Helixi338 – 35417Combined sources
Helixi357 – 3604Combined sources
Beta strandi372 – 3787Combined sources
Turni379 – 3824Combined sources
Beta strandi383 – 3886Combined sources
Turni397 – 3993Combined sources
Helixi400 – 40910Combined sources
Beta strandi412 – 4187Combined sources
Beta strandi427 – 4337Combined sources
Helixi434 – 4363Combined sources
Helixi447 – 4493Combined sources
Beta strandi460 – 4634Combined sources
Helixi473 – 48311Combined sources
Beta strandi487 – 4915Combined sources
Helixi497 – 50610Combined sources
Beta strandi508 – 5169Combined sources
Beta strandi528 – 5314Combined sources
Helixi541 – 5499Combined sources
Beta strandi553 – 56311Combined sources
Turni568 – 5725Combined sources
Beta strandi576 – 5816Combined sources
Helixi586 – 5883Combined sources
Helixi589 – 5979Combined sources
Beta strandi613 – 6153Combined sources
Helixi616 – 6183Combined sources
Beta strandi634 – 6363Combined sources
Turni638 – 6414Combined sources
Helixi645 – 6506Combined sources
Beta strandi668 – 67710Combined sources
Helixi704 – 7074Combined sources
Beta strandi724 – 7274Combined sources
Helixi729 – 7335Combined sources
Turni736 – 7394Combined sources
Helixi742 – 7443Combined sources
Turni748 – 7514Combined sources
Helixi769 – 7724Combined sources
Beta strandi774 – 78411Combined sources
Beta strandi786 – 7883Combined sources
Beta strandi790 – 7923Combined sources
Beta strandi795 – 7995Combined sources
Beta strandi809 – 8135Combined sources
Beta strandi816 – 8183Combined sources
Beta strandi823 – 8319Combined sources
Helixi832 – 8354Combined sources
Beta strandi837 – 8393Combined sources
Turni840 – 8434Combined sources
Beta strandi844 – 8463Combined sources
Beta strandi853 – 8619Combined sources
Beta strandi865 – 8684Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031215.
InParanoidiQ4WJJ3.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG7HMS8F.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
5FJIX-ray1.95A/B30-873[»]
ProteinModelPortaliQ4WJJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei8995. Asp f Glucosidase.
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.
OrthoDBiEOG7HMS8F.

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...

Publicationsi

  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

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: June 8, 2016
This is version 65 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.