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P18336 (GUN_CELUD) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. 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

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
OrganismCellulomonas uda
Taxonomic identifier1714 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Chain24 – 359336Endoglucanase
PRO_0000007933

Sites

Active site531Proton donor By similarity
Active site1101Nucleophile Potential

Sequences

Sequence LengthMass (Da)Tools
P18336 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 0445D7571B683148

FASTA35940,690
        10         20         30         40         50         60 
MPLRALVAVI VTTAVMLVPR AWAQTAWERY KARFMMPDAR IIDTANGNVS HTEGQGFAML 

        70         80         90        100        110        120 
LAVANNDRPA FDKLWQWTDS TLRDKSNGLF YWRYNPVAPD PIADKNNATD GDTLIAWALL 

       130        140        150        160        170        180 
RAQKQWQDKR YATASDAITA SLLKYTVVTF AGRQVMLPGV KGFNRNDHLN LNPSYFIFPA 

       190        200        210        220        230        240 
WRAFAERTHL TAWRTLQSDG QALLGQMGWG KSHLPSDWVA LRADGKMLPA KEWPPRMSFD 

       250        260        270        280        290        300 
AIRIPLYISW VDPHSALLAP WKAWMQSYPR LQTPAWINVS TNEVAPWNMA GGLLAVRDLT 

       310        320        330        340        350 
LGEPLERRRL TTRMIITPPA SSCWSGWRNR ISASAVMALQ VSQPVCLRAE RKEQERLTM 

« Hide

References

[1]"Sequence of a cellulase gene of Cellulomonas uda CB4."
Nakamura K., Misawa N., Kitamura K.
J. Biotechnol. 4:247-254(1986)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-37.
Strain: CB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36503 Genomic DNA. Translation: AAA23090.1.
PIRI40696.

3D structure databases

ProteinModelPortalP18336.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH8. Glycoside Hydrolase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
PfamPF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSPR00735. GLHYDRLASE8.
SUPFAMSSF48208. SSF48208. 1 hit.
PROSITEPS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN_CELUD
AccessionPrimary (citable) accession number: P18336
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 16, 2013
This is version 66 of the entry and version 1 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