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Protein

Endo-beta-1,4-glucanase A

Gene

eglA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: 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.2 Publications

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 57 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei150 – 1501Proton donorBy similarity
Active sitei257 – 2571NucleophileBy 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

mycoCLAPiEGL5A_EMENI.
EGL5B_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-1,4-glucanase A (EC:3.2.1.4)
Short name:
Endoglucanase A
Alternative name(s):
Carboxymethylcellulase A
Cellulase A
Gene namesi
Name:eglA
ORF Names:AN1285
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VIII

Subcellular locationi

  1. 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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 326307Endo-beta-1,4-glucanase APRO_5000049150Add
BLAST

Expressioni

Inductioni

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

Structurei

3D structure databases

ProteinModelPortaliQ5BDU5.
SMRiQ5BDU5. Positions 21-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000111120.
InParanoidiQ5BDU5.
KOiK01179.
OMAiYMYSFEP.
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.

Q5BDU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLVLLSSV LALVAPSKGA FTWLGTNEAG AEFGEGSYPG ELGTEYIWPD
60 70 80 90 100
LGTIGTLRNE GMNIFRVAFS MERLVPDSLA GPVADEYFQD LVETVNGITA
110 120 130 140 150
LGAYAVLDPH NYGRYYGNII TSTDDFAAFW TILATEFASN ELVIFDTNNE
160 170 180 190 200
YHTMDQSLVL NLNQAAIDAI RASGATSQYI FAEGNSWTGA WTWVDVNDNM
210 220 230 240 250
KALTDPQDKL IYEMHQYLDS DGSGTNTACV SSTIGSERVT AATNWLRENG
260 270 280 290 300
KLGVLGEFAG ANNQVCKDAV ADLLEYLEEN SDVWLGALWW AAGPWWGDYM
310 320
FNMEPTSGIA YQEYSEILQP YFVGSQ
Length:326
Mass (Da):35,812
Last modified:April 26, 2005 - v1
Checksum:i7BFED0EF254B8D9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161Missing in BAA82592 (PubMed:10386374).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009402 Genomic DNA. Translation: BAA82592.1.
DQ490472 mRNA. Translation: ABF50848.1.
AACD01000017 Genomic DNA. Translation: EAA65878.1.
BN001308 Genomic DNA. Translation: CBF87793.1.
RefSeqiXP_658889.1. XM_653797.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001335; CADANIAP00001335; CADANIAG00001335.
GeneIDi2877061.
KEGGiani:AN1285.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009402 Genomic DNA. Translation: BAA82592.1.
DQ490472 mRNA. Translation: ABF50848.1.
AACD01000017 Genomic DNA. Translation: EAA65878.1.
BN001308 Genomic DNA. Translation: CBF87793.1.
RefSeqiXP_658889.1. XM_653797.1.

3D structure databases

ProteinModelPortaliQ5BDU5.
SMRiQ5BDU5. Positions 21-322.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiEGL5A_EMENI.
EGL5B_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00001335; CADANIAP00001335; CADANIAG00001335.
GeneIDi2877061.
KEGGiani:AN1285.2.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000111120.
InParanoidiQ5BDU5.
KOiK01179.
OMAiYMYSFEP.
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. "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. 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.
    , 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 nameiEGLA_EMENI
AccessioniPrimary (citable) accession number: Q5BDU5
Secondary accession number(s): C8VSF3, Q1HFV2, Q9Y8H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 26, 2005
Last modified: January 7, 2015
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

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.