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Protein

Endo-beta-1,4-glucanase B

Gene

eglB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 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 4.0.1 Publication

Temperature dependencei

Optimum temperature is 52 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei155 – 1551Proton donorBy similarity
Active sitei262 – 2621NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. glucan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

mycoCLAPiEGL5C_EMENI.

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
ORF Names:AN5214
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome V

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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 328311Endo-beta-1,4-glucanase BPRO_0000394058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00003212.

Structurei

3D structure databases

ProteinModelPortaliQ1HFS8.
SMRiQ1HFS8. Positions 27-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000111120.
InParanoidiQ1HFS8.
KOiK01179.
OrthoDBiEOG776T0S.

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.

Q1HFS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVNTLLVAV AAGTAMAAPQ LKKRAGFTFF GVTEAGAEFG EKSIPGVWGT
60 70 80 90 100
DYTFPDTESI LTLISKGFNT FRIPFLMERL TPEMTGSFDE GYLKNLTSVV
110 120 130 140 150
NAVTDAGAWA IVDAQNFGRF NGEIISSASD FQTWWKNVAA EFADNKNVIF
160 170 180 190 200
DTNNEFHDMD QTLVLDLNQA AINGIRAAGA TSQYIFVEGN SYTGAWTWTD
210 220 230 240 250
NNDNLKSLTD PQDKIVYEMH QYLDTDGSGT HETCVSETIG AERVESATQW
260 270 280 290 300
LKDNGKLGVI GEFAGGNNEI CRAAVKSLLD ALKENDDVWL GALWWAAGPW
310 320
WEDYMFSMEP TDGIAYTGML STLEAYMN
Length:328
Mass (Da):36,080
Last modified:June 13, 2006 - v1
Checksum:i7FBF3D7078476B4D
GO

Sequence cautioni

The sequence CBF81096.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA62395.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490496 mRNA. Translation: ABF50872.1.
AACD01000089 Genomic DNA. Translation: EAA62395.1. Sequence problems.
BN001305 Genomic DNA. Translation: CBF81096.1. Sequence problems.
RefSeqiXP_662818.1. XM_657726.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003212; CADANIAP00003212; CADANIAG00003212.
GeneIDi2871506.
KEGGiani:AN5214.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490496 mRNA. Translation: ABF50872.1.
AACD01000089 Genomic DNA. Translation: EAA62395.1. Sequence problems.
BN001305 Genomic DNA. Translation: CBF81096.1. Sequence problems.
RefSeqiXP_662818.1. XM_657726.1.

3D structure databases

ProteinModelPortaliQ1HFS8.
SMRiQ1HFS8. Positions 27-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00003212.

Protein family/group databases

mycoCLAPiEGL5C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00003212; CADANIAP00003212; CADANIAG00003212.
GeneIDi2871506.
KEGGiani:AN5214.2.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000111120.
InParanoidiQ1HFS8.
KOiK01179.
OrthoDBiEOG776T0S.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "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.

Entry informationi

Entry nameiEGLB_EMENI
AccessioniPrimary (citable) accession number: Q1HFS8
Secondary accession number(s): C8VF90, Q5B2L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: June 13, 2006
Last modified: January 7, 2015
This is version 50 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. 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.