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P07103 (GUNZ_DICD3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 Z

EC=3.2.1.4
Alternative name(s):
Cellulase Z
Endo-1,4-beta-glucanase Z
Short name=EGZ
Gene names
Name:celZ
Synonyms:cel5, cel5Z
Ordered Locus Names:Dda3937_02793
OrganismDickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) [Complete proteome] [HAMAP]
Taxonomic identifier198628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Represents 97% of the global cellulase activity.

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
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_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4343
Chain44 – 426383Endoglucanase Z
PRO_0000007860

Regions

Region44 – 332289Catalytic
Region333 – 36634Linker
Region367 – 42660Cellulose-binding

Sites

Active site1761Proton donor
Active site2631Nucleophile By similarity

Amino acid modifications

Disulfide bond368 ↔ 425 Ref.2

Experimental info

Mutagenesis1411H → A: Loss of activity.
Mutagenesis1761E → A: Loss of activity.
Sequence conflict293 – 2953SNA → QLTQ in CAA68604. Ref.1
Sequence conflict350 – 36415TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604. Ref.1
Sequence conflict388 – 42639THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN Ref.1

Secondary structure

.............................................................. 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07103 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: E78F2EE021FCA5DA

FASTA42646,418
        10         20         30         40         50         60 
MPLSYLDKNP VIDSKKHALR KKLFLSCAYF GLSLACLSSN AWASVEPLSV NGNKIYAGEK 

        70         80         90        100        110        120 
AKSFAGNSLF WSNNGWGGEK FYTADTVASL KKDWKSSIVR AAMGVQESGG YLQDPAGNKA 

       130        140        150        160        170        180 
KVERVVDAAI ANDMYAIIGW HSHSAENNRS EAIRFFQEMA RKYGNKPNVI YEIYNEPLQV 

       190        200        210        220        230        240 
SWSNTIKPYA EAVISAIRAI DPDNLIIVGT PSWSQNVDEA SRDPINAKNI AYTLHFYAGT 

       250        260        270        280        290        300 
HGESLRNKAR QALNNGIALF VTEWGTVNAD GNGGVNQTET DAWVTFMRDN NISNANWALN 

       310        320        330        340        350        360 
DKNEGASTYY PDSKNLTESG KKVKSIIQSW PYKAGSAASA TTDPSTDTTT DTTVDEPTTT 

       370        380        390        400        410        420 
DTPATADCAN ANVYPNWVSK DWAGGQPTHN EAGQSIVYKG NLYTANWYTA SVPGSDSSWT 


QVGSCN 

« Hide

References

« Hide 'large scale' references
[1]"Homology between endoglucanase Z of Erwinia chrysanthemi and endoglucanases of Bacillus subtilis and alkalophilic Bacillus."
Guiseppi A., Cami B., Aymeric J.-L., Ball G., Creuzet N.
Mol. Microbiol. 2:159-164(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 3937.
[2]"Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi."
Bortoli-German I., Brun E., Py B., Chippaux M., Barras F.
Mol. Microbiol. 11:545-553(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, DISULFIDE BOND.
[3]"Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937."
Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N., Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D., Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K., Rauscher L., Rodriguez-Palenzuela P., Toussaint A. expand/collapse author list , Holeva M.C., He S.Y., Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S., Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S., Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M., Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R., Blattner F.R., Keen N.T., Perna N.T.
J. Bacteriol. 193:2076-2077(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 3937.
[4]"Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis."
Py B., Bortoli-German I., Haiech J., Chippaux M., Barras F.
Protein Eng. 4:325-333(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, DOMAINS.
[5]"Stereochemistry of the hydrolysis reaction catalyzed by endoglucanase Z from Erwinia chrysanthemi."
Barras F., Bortoli-German I., Bauzan M., Rouvier J., Gey C., Heyraud A., Henrissat B.
FEBS Lett. 300:145-148(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STEREOCHEMISTRY OF THE REACTION.
Strain: 3937.
[6]"Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi."
Brun E., Moriaud F., Gans P., Blackledge M.J., Barras F., Marion D.
Biochemistry 36:16074-16086(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 365-426.
[7]"Type II protein secretion in Gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi."
Chapon V., Czjzek M., El Hassouni M., Py B., Juy M., Barras F.
J. Mol. Biol. 310:1055-1066(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 44-335.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00540 Genomic DNA. Translation: CAA68604.1.
CP002038 Genomic DNA. Translation: ADM99099.1.
PIRS03767.
RefSeqYP_003883656.1. NC_014500.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIWNMR-A367-426[»]
1EGZX-ray2.30A/B/C44-334[»]
ProteinModelPortalP07103.
SMRP07103. Positions 44-334, 366-426.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADM99099; ADM99099; Dda3937_02793.
GeneID9734341.
KEGGddd:Dda3937_02793.
PATRIC42318137. VBIDicDad25310_2889.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000253566.
KOK01179.
OMAGGEKFYT.

Enzyme and pathway databases

BioCycDDAD198628:GHFQ-2956-MONOMER.

Family and domain databases

Gene3D2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProIPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07103.

Entry information

Entry nameGUNZ_DICD3
AccessionPrimary (citable) accession number: P07103
Secondary accession number(s): E0SIP0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 1994
Last modified: May 14, 2014
This is version 111 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries