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O74706

- EGLB_ASPNG

UniProt

O74706 - EGLB_ASPNG

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Protein
Endo-beta-1,4-glucanase B
Gene
eglB, eng1
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton donor By similarity
Active sitei266 – 2661Nucleophile By 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.
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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 331313Endo-beta-1,4-glucanase B
PRO_5000065052Add
BLAST

Amino acid modifications

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

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131A → G in AAG50051. 1 Publication
Sequence conflicti23 – 231S → P in AAG50051. 1 Publication
Sequence conflicti63 – 631T → A in AAG50051. 1 Publication
Sequence conflicti69 – 691G → D in AAG50051. 1 Publication
Sequence conflicti105 – 1051V → I in AAG50051. 1 Publication
Sequence conflicti117 – 1171I → V in AAG50051. 1 Publication
Sequence conflicti141 – 1411Q → E in AAG50051. 1 Publication
Sequence conflicti162 – 1621Y → H in AAG50051. 1 Publication
Sequence conflicti185 – 1851A → AT in AAG50051. 1 Publication
Sequence conflicti241 – 2411G → E in AAG50051. 1 Publication
Sequence conflicti248 – 2503ITD → VTE in AAG50051. 1 Publication
Sequence conflicti329 – 3291T → A in AAG50051. 1 Publication

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: November 13, 2013
This is version 69 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

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