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Q5BCC6

- BGLC_EMENI

UniProt

Q5BCC6 - BGLC_EMENI

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Protein

Beta-glucosidase C

Gene

bglC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 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.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Optimum temperature is 52 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei330 – 3301By similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
  2. glucan catabolic process Source: UniProtKB
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

mycoCLAPiBGL3C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase C (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase C
Cellobiase C
Gentiobiase C
Gene namesi
Name:bglC
ORF Names:AN1804
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VII

Subcellular locationi

Secreted Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 618599Beta-glucosidase CPRO_0000394105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5BCC6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000285275.
InParanoidiQ5BCC6.
OMAiHWVGYGA.
OrthoDBiEOG7R8394.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF00933. 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.

Q5BCC6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVDSTVLAL VALATDCLGL AIKSNEPELL RRDALPIYKN ASYCVDERVR
60 70 80 90 100
DLLSRMTLEE KAGQLFHKQL SEGPLDDDSS GNSTETMIGK KHMTHFNLAS
110 120 130 140 150
DITNATQTAE FINLIQKRAL QTRLGIPITI STDPRHSFTE NVGTGFQAGV
160 170 180 190 200
FSQWPESLGL AALRDPQLVR EFAEVAREEY LAVGIRAALH PQVDLSTEPR
210 220 230 240 250
WARISGTWGE NSTLTSELIV EYIKGFQGEG KLGPKSVKTV TKHFPGGGPM
260 270 280 290 300
ENGEDSHFYY GKNQTYPGNN IDEHLIPFKA ALAAGATEIM PYYSRPIGTN
310 320 330 340 350
WEAVGFSFNK EIVTDLLRGE LGFDGIVLTD WGLITDTYIG NQYMPARAWG
360 370 380 390 400
VEYLSELQRA ARILDAGCDQ FGGEERPELI VQLVREGTIS EDRIDVSVAR
410 420 430 440 450
LLKEKFLLGL FDNPFVNASA ANNIVGNEHF VNLGRDAQRR SYTLLTNNQT
460 470 480 490 500
ILPLAKPGEG TRFYIEGFDS AFMSARNYTV VNTTEEADFA LLRYNAPYEP
510 520 530 540 550
RNGTFEANFH AGSLAFNATE KARQAKIYSS LPTIVDIILD RPAVIPEVVE
560 570 580 590 600
QAQAVLASYG SDSEAFLDVV FGVSKPEGKL PFDLPRSMDA VEAQAEDLPF
610
DTENPVFRYG HGLEYEDN
Length:618
Mass (Da):68,420
Last modified:April 26, 2005 - v1
Checksum:i478BEDD19CF97756
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACD01000029 Genomic DNA. Translation: EAA64969.1.
BN001307 Genomic DNA. Translation: CBF85593.1.
RefSeqiXP_659408.1. XM_654316.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008452; CADANIAP00008452; CADANIAG00008452.
GeneIDi2874927.
KEGGiani:AN1804.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACD01000029 Genomic DNA. Translation: EAA64969.1 .
BN001307 Genomic DNA. Translation: CBF85593.1 .
RefSeqi XP_659408.1. XM_654316.1.

3D structure databases

ProteinModelPortali Q5BCC6.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

mycoCLAPi BGL3C_EMENI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00008452 ; CADANIAP00008452 ; CADANIAG00008452 .
GeneIDi 2874927.
KEGGi ani:AN1804.2.

Phylogenomic databases

eggNOGi COG1472.
HOGENOMi HOG000285275.
InParanoidi Q5BCC6.
OMAi HWVGYGA.
OrthoDBi EOG7R8394.

Enzyme and pathway databases

UniPathwayi UPA00696 .

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProi IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR30620. PTHR30620. 1 hit.
Pfami PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view ]
PRINTSi PR00133. GLHYDRLASE3.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiBGLC_EMENI
AccessioniPrimary (citable) accession number: Q5BCC6
Secondary accession number(s): C8VPG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 55 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