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Q5B7R2 (CELB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 57. 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 celB

Short name=Endoglucanase celB
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase celB
Cellulase B
Gene names
Name:celB
Synonyms:eglB, eglC
ORF Names:AN3418
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 length430 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.4

Catalytic activity

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

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Ref.4

Temperature dependence:

Optimum temperature is 42 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   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.4. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 430414Endo-beta-1,4-glucanase celB
PRO_0000395159

Sites

Active site2161Nucleophile By similarity
Active site2211Proton donor By similarity

Amino acid modifications

Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict451S → Y in AAM54071. Ref.1
Sequence conflict731P → R in AAM54071. Ref.1
Sequence conflict1131N → Y in AAM54071. Ref.1
Sequence conflict1531N → Y in AAM54071. Ref.1
Sequence conflict3161E → D in AAM54071. Ref.1
Sequence conflict3451C → W in AAM54071. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5B7R2 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 4807FA907F18749E

FASTA43045,929
        10         20         30         40         50         60 
MALLLSLSLL ATTISAQQIG TPEIRPRLTT YHCTSANGCT EQNTSVVLDA ATHPIHDASN 

        70         80         90        100        110        120 
PSVSCTTSNG LNPALCPDKQ TCADNCVIDG ITDYAAHGVE THGSRLTLTQ YRNVNGALSS 

       130        140        150        160        170        180 
VSPRVYLVDE SDPDEQEYRA LSLLAQEFTF TVNVSALPCG MNGALYLSEM SPSGGRSALN 

       190        200        210        220        230        240 
PAGASYGTGY CDAQCYVNPW INGEGNINGY GACCNEMDIW EANSRSTGFT PHACLYEPEE 

       250        260        270        280        290        300 
TEGRGVYECA SEDECDSAGE NDGICDKWGC GFNPYALGNT EYYGRGQGFE VDTKEPFTVV 

       310        320        330        340        350        360 
TQFLTDDGTS TGALTEIRRL YIQNGQVIEN AVVSSGADSL TDSLCASTAS WFDSYGGMEG 

       370        380        390        400        410        420 
MGRALGRGMV LAMSIWNDAG GYMQWLDGGD AGPCNATEGA PEFIEEHTPW TRVVFEDLKW 

       430 
GDIGSTFQAS 

« Hide

References

« Hide 'large scale' references
[1]"Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans."
Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M.
Fungal Genet. Biol. 37:190-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[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. 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.
[4]"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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF420021 Genomic DNA. Translation: AAM54071.1.
AACD01000055 Genomic DNA. Translation: EAA63386.1.
BN001306 Genomic DNA. Translation: CBF82749.1.
RefSeqXP_661022.1. XM_655930.1.

3D structure databases

ProteinModelPortalQ5B7R2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00009621.

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7A_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00009621; CADANIAP00009621; CADANIAG00009621.
GeneID2874128.
KEGGani:AN3418.2.

Phylogenomic databases

eggNOGNOG138370.
HOGENOMHOG000182210.
OMAPWINGEA.
OrthoDBEOG7Q8CXJ.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCELB_EMENI
AccessionPrimary (citable) accession number: Q5B7R2
Secondary accession number(s): C8VHK3, Q8NK01
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: March 19, 2014
This is version 57 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