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Protein

Probable beta-glucosidase btgE

Gene

btgE

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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.

Pathway: 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 sitei538 – 5381NucleophileBy similarity
Active sitei592 – 5921Proton donorBy 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-glucosidase btgE (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase btgE
Cellobiase btgE
Gentiobiase btgE
Gene namesi
Name:btgE
ORF Names:AO090005000582
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 1

Subcellular locationi

  • Secretedcell wall By similarity

  • Note: Covalently-linked to the cell wall.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 602584Probable beta-glucosidase btgEPRO_0000395134Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00002524.

Structurei

3D structure databases

ProteinModelPortaliQ2US39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 321228Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000158427.
OMAiYSTDCDT.
OrthoDBiEOG73FQWG.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q2US39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGAFLAAAA AVAGTAMADV AHMRRHGHDS FHHNRAYQPE VPAEGDENCE
60 70 80 90 100
CTTKVITITG PPTLVPINTP APEPSSSSSS EVPSVPSSES SVVTSEAVTT
110 120 130 140 150
LHSTSTATVT VVTTPGVDAT GAQTPTGGVP GTPEASSPAG TPEASTPAVP
160 170 180 190 200
ATSESPLPTP GVTSFSSTGI YTIPATTVTV RDTTTVCGAT TTELPSGTHT
210 220 230 240 250
FGGVTTVVST ATTVTCPVAT VEPSGSTVTS KIYTTTYVCP SAGTYTIAPT
260 270 280 290 300
TTYVPTSTVV VYPTPATITP GTYTQDEQTV TVTRTDFTYV CPFTGNDQPT
310 320 330 340 350
SAPVASTSAV PVTTTAAPST TSAVASSSAS ASSTATAVPT GVSGQQMGMT
360 370 380 390 400
YSPYTNEGGC QSKDQVLKDV ALIKQKGFTH VRVYSTDCNG LEYIGEAARE
410 420 430 440 450
NGLKMIIGVF ISSTGISGAQ EQVTAITKWA QWDLVTLVVV GNEAIQNGYT
460 470 480 490 500
DASSLAGFIS SCKSSFQASG YSGQVTTTEP INVWQQSGSA LCGAVDILGA
510 520 530 540 550
NLHPFFNADV TPDQAGSFVR AQIKDLEAVC NKDVINLETG WPSAGNANGK
560 570 580 590 600
AVPGTAQQAA AIKALVEEVG SQSVFFSYSN DLWKDAGEFD VERYWGCIDQ

FK
Length:602
Mass (Da):61,824
Last modified:January 24, 2006 - v1
Checksum:i94BCCF3A057E95D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007151 Genomic DNA. Translation: BAE55626.1.

Genome annotation databases

EnsemblFungiiCADAORAT00002562; CADAORAP00002524; CADAORAG00002562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007151 Genomic DNA. Translation: BAE55626.1.

3D structure databases

ProteinModelPortaliQ2US39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00002524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00002562; CADAORAP00002524; CADAORAG00002562.

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000158427.
OMAiYSTDCDT.
OrthoDBiEOG73FQWG.

Enzyme and pathway databases

UniPathwayiUPA00696.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiBTGE_ASPOR
AccessioniPrimary (citable) accession number: Q2US39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: April 1, 2015
This is version 51 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, 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. 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.