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Q01786 (GUN5_THEFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Endoglucanase E-5

EC=3.2.1.4
Alternative name(s):
Cellulase E-5
Cellulase E5
Endo-1,4-beta-glucanase E-4
Gene names
Name:celE
OrganismThermobifida fusca (Thermomonospora fusca)
Taxonomic identifier2021 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Sequence similarities

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

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636
Chain37 – 466430Endoglucanase E-5
PRO_0000007866

Regions

Domain37 – 139103CBM2

Sites

Active site2991Proton donor By similarity
Active site3911Nucleophile By similarity

Secondary structure

......................................................... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01786 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 1CF0ADFBF2DEF82E

FASTA46649,801
        10         20         30         40         50         60 
MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD NGYSASVTVR 

        70         80         90        100        110        120 
NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT GVSWNSTIPP GGTASSGFIA 

       130        140        150        160        170        180 
SGSGEPTHCT INGAPCDEGS EPGGPGGPGT PSPDPGTQPG TGTPVERYGK VQVCGTQLCD 

       190        200        210        220        230        240 
EHGNPVQLRG MSTHGIQWFD HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD 

       250        260        270        280        290        300 
RMHQLIDMAT ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP 

       310        320        330        340        350        360 
NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA ANPVNASNIM 

       370        380        390        400        410        420 
YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD GANDFQMADR YIDLMAERKI 

       430        440        450        460 
GWTKWNYSDD FRSGAVFQPG TCASGGPWSG SSLKASGQWV RSKLQS 

« Hide

References

[1]"DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora fusca."
Lao G., Ghangas G.S., Jung E.D., Wilson D.B.
J. Bacteriol. 173:3397-3407(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YX.
[2]Lao G., Ghangas G.S., Jung E.D., Wilson D.B.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects."
Irwin D.C., Spezio M., Walker L.P., Wilson D.B.
Biotechnol. Bioeng. 42:1002-1013(1993)
Cited for: PROTEIN SEQUENCE OF 137-142 AND 157-166.
Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01577 Genomic DNA. Translation: AAC09379.1.
PIRC42360.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKRX-ray1.77A/B161-466[»]
2CKSX-ray1.60A/B161-466[»]
ProteinModelPortalQ01786.
SMRQ01786. Positions 161-466.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01786.

Entry information

Entry nameGUN5_THEFU
AccessionPrimary (citable) accession number: Q01786
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1999
Last modified: December 11, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries