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Q59394 (GUNN_PECAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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 N

EC=3.2.1.4
Alternative name(s):
Cellulase N
Endo-1,4-beta-glucanase N
Gene names
Name:celN
OrganismPectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica)
Taxonomic identifier29471 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subcellular location

Secreted.

Sequence similarities

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

Contains 1 CBM3 (carbohydrate binding type-3) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
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 – 3131 Potential
Chain32 – 444413Endoglucanase N
PRO_0000007857

Regions

Domain356 – 44489CBM3

Sites

Active site1681Proton donor By similarity
Active site2561Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59394 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FA7E4179004CBB43

FASTA44448,301
        10         20         30         40         50         60 
MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD EQGKRVQLRG 

        70         80         90        100        110        120 
VSSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG YISNPSLANK VKEAVAAAQS 

       130        140        150        160        170        180 
LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE MAGLYGSSPN VIYEIANEPN GGVTWNGQIR 

       190        200        210        220        230        240 
PYALEVTDTI RSKDPDNLII VGTGTWSQDI HDAADNQLPD PNTLYALHFY AGTHGQFLRD 

       250        260        270        280        290        300 
RIDYAQSRGA AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA 

       310        320        330        340        350        360 
ALAPGASKSG GWTEQNLSTS GKFVREQIRA GANLGGGDTP TTPTTPTEPT NPGNGTTGDV 

       370        380        390        400        410        420 
VLQYRNVDNN PSDDAIRMAV NIKNTGSTPI KLSDLQVRYY FHDDGKPGAN LFVDWANVGP 

       430        440 
NNIVTSTGTP AASTDKANRY VLVT 

« Hide

References

[1]"Transplanting two unique beta-glucanase catalytic activities into one multienzyme, which forms glucose."
Olsen O., Thomsen K.K., Weber J., Duus J.O., Svendsen I., Wegener C., von Wettstein D.
Biotechnology (N.Y.) 14:71-76(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39788 Genomic DNA. Translation: AAC37033.1.

3D structure databases

ProteinModelPortalQ59394.
SMRQ59394. Positions 35-332.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2730.

Family and domain databases

Gene3D2.60.40.710. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00942. CBM_3. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51172. CBM3. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNN_PECAT
AccessionPrimary (citable) accession number: Q59394
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 82 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