Skip Header

Contribute Send feedback
Read comments (?) or add your own

P26222 (GUN2_THEFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. 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
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-2
EC=3.2.1.4
Alternative name(s):
Cellulase E-2
Cellulase E2
Endo-1,4-beta-glucanase E-2
Gene names
Name:celB
OrganismThermomonospora fusca
Taxonomic identifier2021 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Nocardiopsaceae › Thermobifida

Protein attributes

Sequence length441 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.

Subunit structure

Homodimer. Ref.4

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the glycosyl hydrolase 6 (cellulase B) family.

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   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: 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 – 3131Tat-type signal Ref.3
Chain32 – 441410Endoglucanase E-2
PRO_0000007909

Regions

Domain339 – 441103CBM2
Region32 – 320289Catalytic
Region321 – 34020Linker

Sites

Active site1101
Active site1481Proton donor
Active site2961Nucleophile

Amino acid modifications

Disulfide bond111 ↔ 156
Disulfide bond263 ↔ 298
Disulfide bond346 ↔ 438 Potential

Experimental info

Mutagenesis1631E → G: Loss of ability to form dimers. Ref.4

Secondary structure

1 .................................................. 441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26222 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 87218E4537092AE5

FASTA44145,844
        10         20         30         40         50         60 
MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN NPNDPRTPVI 

        70         80         90        100        110        120 
RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI LVVYNAPGRD CGNHSSGGAP 

       130        140        150        160        170        180 
SHSAYRSWID EFAAGLKNRP AYIIVEPDLI SLMSSCMQHV QQEVLETMAY AGKALKAGSS 

       190        200        210        220        230        240 
QARIYFDAGH SAWHSPAQMA SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG 

       250        260        270        280        290        300 
NPSLRAVIDT SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA 

       310        320        330        340        350        360 
GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY TIANEWNDGF 

       370        380        390        400        410        420 
QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS SVTARNVGHN GTLSQGASTE 

       430        440 
FGFVGSKGNS NSVPTLTCAA S

« 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]Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B.
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
Strain: YX.
[3]"Cellulases of Thermomonospora fusca."
Wilson D.B.
Methods Enzymol. 160:314-323(1988)
Cited for: PROTEIN SEQUENCE OF 32-47.
[4]"Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2."
McGinnis K., Kroupis C., Wilson D.B.
Biochemistry 32:8146-8150(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF GLU-163.
[5]"Crystal structure of the catalytic domain of a thermophilic endocellulase."
Spezio M., Wilson D.B., Karplus P.A.
Biochemistry 32:9906-9916(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M73321 mRNA. Translation: AAC06388.1.
PIRA42360.
T12011.
RefSeqYP_289135.1. NC_007333.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMLX-ray1.80A32-317[»]
2BODX-ray1.50X32-317[»]
2BOEX-ray1.15X32-317[»]
2BOFX-ray1.64X32-317[»]
2BOGX-ray1.04X32-317[»]
3RPTX-ray1.30A/X33-317[»]
ProteinModelPortalP26222.
SMRP26222. Positions 32-317.
ModBaseSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3580066.
KEGGtfu:Tfu_1074.

Phylogenomic databases

KOK01179.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSPR00733. GLHYDRLASE6.
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. Cellul_bind. 1 hit.
SSF51989. Glyco_hydro_6. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26222.

Entry information

Entry nameGUN2_THEFU
AccessionPrimary (citable) accession number: P26222
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents