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Q5BDU5 (EGLA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-beta-1,4-glucanase A

Short name=Endoglucanase A
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase A
Cellulase A
Gene names
Name:eglA
ORF Names:AN1285
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

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

Subcellular location

Secreted By similarity.

Induction

Highly expressed in presence of carboxymethylcellulose (CMC). Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.0. Ref.2

Temperature dependence:

Optimum temperature is 57 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

glucan catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 326307Endo-beta-1,4-glucanase A
PRO_5000049150

Sites

Active site1501Proton donor By similarity
Active site2571Nucleophile By similarity

Experimental info

Sequence conflict1161Missing in BAA82592. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5BDU5 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 7BFED0EF254B8D9F

FASTA32635,812
        10         20         30         40         50         60 
MRSLVLLSSV LALVAPSKGA FTWLGTNEAG AEFGEGSYPG ELGTEYIWPD LGTIGTLRNE 

        70         80         90        100        110        120 
GMNIFRVAFS MERLVPDSLA GPVADEYFQD LVETVNGITA LGAYAVLDPH NYGRYYGNII 

       130        140        150        160        170        180 
TSTDDFAAFW TILATEFASN ELVIFDTNNE YHTMDQSLVL NLNQAAIDAI RASGATSQYI 

       190        200        210        220        230        240 
FAEGNSWTGA WTWVDVNDNM KALTDPQDKL IYEMHQYLDS DGSGTNTACV SSTIGSERVT 

       250        260        270        280        290        300 
AATNWLRENG KLGVLGEFAG ANNQVCKDAV ADLLEYLEEN SDVWLGALWW AAGPWWGDYM 

       310        320 
FNMEPTSGIA YQEYSEILQP YFVGSQ 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression properties of the endo-beta-1,4-glucanase A gene from the filamentous fungus Aspergillus nidulans."
Chikamatsu G., Shirai K., Kato M., Kobayashi T., Tsukagoshi N.
FEMS Microbiol. Lett. 175:239-245(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
[2]"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.
[3]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB009402 Genomic DNA. Translation: BAA82592.1.
DQ490472 mRNA. Translation: ABF50848.1.
AACD01000017 Genomic DNA. Translation: EAA65878.1.
BN001308 Genomic DNA. Translation: CBF87793.1.
RefSeqXP_658889.1. XM_653797.1.

3D structure databases

ProteinModelPortalQ5BDU5.
SMRQ5BDU5. Positions 21-322.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

mycoCLAPEGL5A_EMENI.
EGL5B_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001335; CADANIAP00001335; CADANIAG00001335.
GeneID2877061.
KEGGani:AN1285.2.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000111120.
KOK01179.
OMAFEPPSGT.
OrthoDBEOG776T0S.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameEGLA_EMENI
AccessionPrimary (citable) accession number: Q5BDU5
Secondary accession number(s): C8VSF3, Q1HFV2, Q9Y8H6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 26, 2005
Last modified: January 22, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries