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O74706

- EGLB_ASPNG

UniProt

O74706 - EGLB_ASPNG

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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

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
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEGL5B_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-KW
Complete GO annotation...

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

        10         20         30         40         50
MKFQSTLLLA AAAGSALAVP HGSGHKKRAS VFEWFGSNES GAEFGTNIPG
60 70 80 90 100
VWGTDYIFPD PSTISTLIGK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN
110 120 130 140 150
LTTVVKAVTD GGAHALIDPH NYGRYNGEII SSTSDFQTFW QNLAGQYKDN
160 170 180 190 200
DLVMFDTNNE YYDMDQDLVL NLNQAAINGI RAAGASQYIF VEGNSWTGAW
210 220 230 240 250
TWVDVNDNMK NLTDPEDKIV YEMHQYLDSD GSGTSETCVS GTIGKERITD
260 270 280 290 300
ATQWLKDNKK VGFIGEYAGG SNDVCRSAVS GMLEYMANNT DVWKGASWWA
310 320 330
AGPWWGDYIF SLEPPDGTAY TGMLDILETY L
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 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: November 26, 2014
This is version 72 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