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Protein

Probable beta-glucosidase L

Gene

bglL

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521By similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-glucosidase L (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase L
Cellobiase L
Gentiobiase L
Gene namesi
Name:bglL
ORF Names:AFUB_091720
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 739722Probable beta-glucosidase LPRO_0000394899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliB0YB65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031215.
OrthoDBiEOG7HMS8F.
PhylomeDBiB0YB65.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.

Sequencei

Sequence statusi: Complete.

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

B0YB65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTLFLSLLA AAVTVHAYGS GGSNWDQAYS RAKDALQKLN QTEKVGLVTG
60 70 80 90 100
VKWMGGPCVG NTYKPESIDY PSLCLQDSPL GIRFANPVTA FPAGINAGAT
110 120 130 140 150
WDTQLLYARG AAMGAEAKGL GIHVQLGPVA GPLGKNPNGG RNWEGFSVDP
160 170 180 190 200
YLSGVAMEKT IRGMQDSGVQ ACAKHWLGNE QEHYRDTISS NIGDRAAHEL
210 220 230 240 250
YVWPFMDAVK AGVASVMCSY NKVNGTWACE SDALNNKLMK EELGFPGYIM
260 270 280 290 300
SDWNAQHSTV NSAVSGLDMT MPGSDFSNPP GSIFWGSNLE AAVADGSVPQ
310 320 330 340 350
SRLDDMVTRI LAAWYLVGQD QGYPPVAFSS WNGGKANVDV TADHGTVARA
360 370 380 390 400
VARDSIVLLK NGHGTLPLRK PKSLAIVGSD AIVNPAGPNA CSDRGCNNGT
410 420 430 440 450
LAMGWGSGTA EFPYLVGPLD AIQKRAAADG TKIVPSTTDD PTAGASAAAA
460 470 480 490 500
AETAIVFINS DSGEGYITVE GNLGDRNNLD PWHNGNELVK AVAAASKNVI
510 520 530 540 550
VVIHSVGPII LETILAQPSV KAIVWAGLPG QESGNALVDV IYGDTTPSGK
560 570 580 590 600
LPYTIAKQAA DYGASWINAE TDDFPEGLYV DYRHFDAKGI APRYEFGYGL
610 620 630 640 650
SYTTFKYSGL WVNMDASAGA ANGQVVPGGP ADLFEVVGQV SVSVRNNGRV
660 670 680 690 700
AGAEVAQLYL GLPDSAPATP PKQLRGFQKL MLQPGQTGRA TFKLTRRDLS
710 720 730
YWDVQQQKWV VPSGTFKVYV GSSSRDIREE GSFRVRRGW
Length:739
Mass (Da):78,411
Last modified:April 8, 2008 - v1
Checksum:iDCD971ABB66B7254
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499601 Genomic DNA. Translation: EDP48455.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00009085; CADAFUBP00008919; CADAFUBG00009085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499601 Genomic DNA. Translation: EDP48455.1.

3D structure databases

ProteinModelPortaliB0YB65.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00009085; CADAFUBP00008919; CADAFUBG00009085.

Phylogenomic databases

HOGENOMiHOG000031215.
OrthoDBiEOG7HMS8F.
PhylomeDBiB0YB65.

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.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiBGLL_ASPFC
AccessioniPrimary (citable) accession number: B0YB65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 8, 2008
Last modified: January 7, 2015
This is version 34 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

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.