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Q96WQ9 (EGLD_ASPKW) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 44. 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:
Probable endo-beta-1,4-glucanase D

Short name=Endoglucanase D
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase D
Cellulase 61A
Cellulase D
Gene names
Name:eglD
Synonyms:cel61A
ORF Names:AKAW_08531
OrganismAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi) [Complete proteome]
Taxonomic identifier1033177 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 408388Probable endo-beta-1,4-glucanase D
PRO_0000394064

Regions

Domain369 – 40537CBM1
Region21 – 237217Catalytic
Region238 – 25417Ser/Thr-rich linker

Sites

Active site1671Proton donor By similarity
Active site2131Nucleophile Potential

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Disulfide bond377 ↔ 394 By similarity
Disulfide bond388 ↔ 404 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96WQ9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: B7CA86C9019F0089

FASTA40841,650
        10         20         30         40         50         60 
MKTTTYSLLA LAAASKLASA HTTVQAVWIN GEDQGLGNTD DGYIRSPPSN SPVTDVTSTD 

        70         80         90        100        110        120 
MTCNVNGDQA ASKTLSVKAG DVVTFEWHHS DRSDSDDIIA SSHKGPVQVY MAPTAKGSNG 

       130        140        150        160        170        180 
NNWVKIAEDG YHKSSDEWAT DILIANKGKH NITVPDVPAG NYLFRPEIIA LHEGNREGGA 

       190        200        210        220        230        240 
QFYMECVQFK VTSDGSNELP SGVSIPGVYT ATDPGILFDI YNSFDSYPIP GPDVWDGSSS 

       250        260        270        280        290        300 
GSSSSGSSSA AVSSAAAAAT TSAVAATTPA TQAAVEVSSS AAAATTEAAA PVVSSAAPVQ 

       310        320        330        340        350        360 
QATSAVTSQA QAAPTTFATS SKKSSKTACK NKTKSNSQVA AATSSVVAPA ATSSVVPVVS 

       370        380        390        400 
ASASASAGGV AKQYERCGGI NHTGPTTCES GSVCKKWNPY YYQCVASQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of endoglucanase genes from an industrial fungus, Aspergillus kawachii."
Hara Y., Hinoki Y., Shimoi H., Ito K.
Biosci. Biotechnol. Biochem. 67:2010-2013(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NBRC 4308.
[2]"Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu."
Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.
Eukaryot. Cell 10:1586-1587(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 4308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB055432 Genomic DNA. Translation: BAB62318.1.
DF126473 Genomic DNA. Translation: GAA90417.1.

3D structure databases

ProteinModelPortalQ96WQ9.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH61. Glycoside Hydrolase Family 61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

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]
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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_ASPKW
AccessionPrimary (citable) accession number: Q96WQ9
Secondary accession number(s): G7XU08
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: December 1, 2001
Last modified: November 13, 2013
This is version 44 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