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Q5BCX8 (EGLD_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 63. 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 D

Short name=Endoglucanase D
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase D
Cellulase D
Gene names
Name:eglD
ORF Names:AN1602
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 length357 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

Catalytic activity

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

Subcellular location

Secreted By similarity.

Domain

Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similarities

Belongs to the glycosyl hydrolase 61 family.

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is under 6.0. Ref.1

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   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.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from direct assay Ref.1. Source: UniProtKB

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 357339Endo-beta-1,4-glucanase D
PRO_0000394067

Regions

Domain319 – 35537CBM1
Region19 – 234216Catalytic
Region235 – 31884Ser/Thr-rich linker

Sites

Active site1631Proton donor By similarity
Active site2091Nucleophile By similarity

Amino acid modifications

Disulfide bond327 ↔ 344 By similarity
Disulfide bond338 ↔ 354 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BCX8 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 64BAB1984CDB49BD

FASTA35736,732
        10         20         30         40         50         60 
MKFSSVLALA ASAKLVASHA TVFAVWINDE DQGLGNTADG YIRTPPNNSP VTDVTSTDLT 

        70         80         90        100        110        120 
CNVNGDQAAA KTLEVAAGDK ITFEWHHNSR DSSDDIIADS HKGPVLVYMA PTEAGSAGKN 

       130        140        150        160        170        180 
WVKIYEDGYN DGTWAVDTLI ANKGKHSVTV PDVPAGNYLF RPEIIALHEG NREGGAQLYM 

       190        200        210        220        230        240 
ECVQFKVTSD GTTQLPEGVS LPGAYTATDE GILFDIYSSF DSYPIPGPAV WDGASSGSGS 

       250        260        270        280        290        300 
SGSGSSSSAA ATSSAEKTAT STTAAATTTA VATSTSSATQ VQPTSVATFT TSVRPTTSAA 

       310        320        330        340        350 
PTTSAPTSSA APTGGTGTGS IQIYQQCGGM NYKGATGCAS GLTCKQWNPY YHQCVQA 

« Hide

References

« Hide 'large scale' references
[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]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490474 mRNA. Translation: ABF50850.1.
AACD01000026 Genomic DNA. Translation: EAA64722.1.
BN001307 Genomic DNA. Translation: CBF85202.1.
RefSeqXP_659206.1. XM_654114.1.

3D structure databases

ProteinModelPortalQ5BCX8.
SMRQ5BCX8. Positions 322-355.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

mycoCLAPPMO9A_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008239; CADANIAP00008239; CADANIAG00008239.
GeneID2875535.
KEGGani:AN1602.2.

Phylogenomic databases

eggNOGNOG120437.
HOGENOMHOG000158937.
OMAGYIDSPP.
OrthoDBEOG7KM64H.

Family and domain databases

InterProIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEGLD_EMENI
AccessionPrimary (citable) accession number: Q5BCX8
Secondary accession number(s): C8VN99, Q1HFV0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 26, 2005
Last modified: January 22, 2014
This is version 63 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