Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O74706

- EGLB_ASPNG

UniProt

O74706 - EGLB_ASPNG

Protein

Endo-beta-1,4-glucanase B

Gene

eglB

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.1 Publication

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei160 – 1601Proton donorBy similarity
    Active sitei266 – 2661NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEGL5A_ASPNG.
    EGL5B_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-beta-1,4-glucanase B (EC:3.2.1.4)
    Short name:
    Endoglucanase B
    Alternative name(s):
    Carboxymethylcellulase B
    Cellulase B
    Gene namesi
    Name:eglB
    Synonyms:eng1
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 331313Endo-beta-1,4-glucanase BPRO_5000065052Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    Expression is under the control of the xylanolytic transcriptional activator xlnR.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00006047.

    Structurei

    3D structure databases

    ProteinModelPortaliO74706.
    SMRiO74706. Positions 31-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O74706-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFQSTLLLA AAAGSALAVP HGSGHKKRAS VFEWFGSNES GAEFGTNIPG    50
    VWGTDYIFPD PSTISTLIGK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN 100
    LTTVVKAVTD GGAHALIDPH NYGRYNGEII SSTSDFQTFW QNLAGQYKDN 150
    DLVMFDTNNE YYDMDQDLVL NLNQAAINGI RAAGASQYIF VEGNSWTGAW 200
    TWVDVNDNMK NLTDPEDKIV YEMHQYLDSD GSGTSETCVS GTIGKERITD 250
    ATQWLKDNKK VGFIGEYAGG SNDVCRSAVS GMLEYMANNT DVWKGASWWA 300
    AGPWWGDYIF SLEPPDGTAY TGMLDILETY L 331
    Length:331
    Mass (Da):36,559
    Last modified:November 1, 1998 - v1
    Checksum:iF3AE4BF70007C707
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131A → G in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti23 – 231S → P in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti63 – 631T → A in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti69 – 691G → D in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti105 – 1051V → I in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti117 – 1171I → V in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti141 – 1411Q → E in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti162 – 1621Y → H in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti185 – 1851A → AT in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti241 – 2411G → E in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti248 – 2503ITD → VTE in AAG50051. (PubMed:16233124)Curated
    Sequence conflicti329 – 3291T → A in AAG50051. (PubMed:16233124)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GQ292753 Genomic DNA. Translation: ACT68011.1.
    AF331518 mRNA. Translation: AAG50051.1.
    AJ224452 Genomic DNA. Translation: CAA11965.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GQ292753 Genomic DNA. Translation: ACT68011.1 .
    AF331518 mRNA. Translation: AAG50051.1 .
    AJ224452 Genomic DNA. Translation: CAA11965.1 .

    3D structure databases

    ProteinModelPortali O74706.
    SMRi O74706. Positions 31-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00006047.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EGL5A_ASPNG.
    EGL5B_ASPNG.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG2730.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger."
      van Peij N.N., Gielkens M.M., de Vries R.P., Visser J., de Graaff L.H.
      Appl. Environ. Microbiol. 64:3615-3619(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
    2. "Cloning of a gene encoding a highly stable endo-beta-1,4-glucanase from Aspergillus niger and its expression in yeast."
      Hong J., Tamaki H., Akiba S., Yamamoto K., Kumagai H.
      J. Biosci. Bioeng. 92:434-441(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: IFO 31125.
    3. Hsing-Ren W., Trong-Rong Y.
      Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BCRC 31494.

    Entry informationi

    Entry nameiEGLB_ASPNG
    AccessioniPrimary (citable) accession number: O74706
    Secondary accession number(s): Q9C3Z7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3