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P27035 (GUNA_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 84. 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:
Endoglucanase CelA

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:celA
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length459 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.

Post-translational modification

The linker region (also termed "hinge") may be a potential site for proteolysis.

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
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 2727 Ref.1
Chain28 – 459432Endoglucanase CelA
PRO_0000007873

Regions

Domain28 – 134107CBM2
Region136 – 14712Linker ("hinge") (Pro-Thr box)
Region148 – 357210Catalytic

Sites

Active site2861Proton donor By similarity
Active site3781Nucleophile By similarity

Amino acid modifications

Disulfide bond31 ↔ 131 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27035 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: CFF47EC34E2F97A7

FASTA45948,663
        10         20         30         40         50         60 
MKRLLALLAT GVSIVGLTAL AGPPAQAATG CKAEYTITSQ WEGGFQAGVK ITNLGDPVSG 

        70         80         90        100        110        120 
WTLGFTMPDA GQRLVQGWNA TWSQSGSAVT AGGVDWNRTL ATGASADLGF VGSFTGANPA 

       130        140        150        160        170        180 
PTSFTLNGAT CSGSVTDPPT DPPTDPPATG TPAAVNGQLH VCGVHLCNQY DRPIQLRGMS 

       190        200        210        220        230        240 
THGIQWFGPC YGDASLDRLA QDWKSDLLRV AMYVQEDGYE TDPAGFTSRV NGLVDMAEDR 

       250        260        270        280        290        300 
GMYAVIDFHT LTPGDPNYNL DRARTFFSSV AARNDKKNVI YEIANEPNGV SWTAVKSYAE 

       310        320        330        340        350        360 
QVIPVIRAAD PDAVVIVGTR GWSSLGVSDG ANESEVVNNP VNATNIMYAF HFYAASHKDD 

       370        380        390        400        410        420 
YRAAVRPAAT RLPLFVSEFG TVSATAWSVD RSSSVAWLDL LDQLKISYAN WTYSDADEGS 

       430        440        450 
AAFRPGTCEG TDYSSSGVLT ESGALVKSRI STTDDFPTS 

« Hide

References

[1]"Purification and characterization of an endoglucanase from Streptomyces lividans 66 and DNA sequence of the gene."
Theberge M., Lacaze P., Shareck F., Morosoli R., Kluepfel D.
Appl. Environ. Microbiol. 58:815-820(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-43.
Strain: 66 / 1326.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M82807 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP27035.
SMRP27035. Positions 150-451.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR018366. CBM2_CS.
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.
PS00561. CBM2_A. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_STRLI
AccessionPrimary (citable) accession number: P27035
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 1992
Last modified: October 16, 2013
This is version 84 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries