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P07103

- GUNZ_DICD3

UniProt

P07103 - GUNZ_DICD3

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Protein
Endoglucanase Z
Gene
celZ, cel5, cel5Z, Dda3937_02793
Organism
Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Represents 97% of the global cellulase activity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei176 – 1761Proton donor
Active sitei263 – 2631Nucleophile By similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciDDAD198628:GHFQ-2956-MONOMER.

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase Z (EC:3.2.1.4)
Alternative name(s):
Cellulase Z
Endo-1,4-beta-glucanase Z
Short name:
EGZ
Gene namesi
Name:celZ
Synonyms:cel5, cel5Z
Ordered Locus Names:Dda3937_02793
OrganismiDickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Taxonomic identifieri198628 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya
ProteomesiUP000006859: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411H → A: Loss of activity.
Mutagenesisi176 – 1761E → A: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343
Add
BLAST
Chaini44 – 426383Endoglucanase Z
PRO_0000007860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi368 ↔ 4251 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 514
Beta strandi54 – 574
Beta strandi65 – 717
Helixi78 – 814
Helixi84 – 929
Beta strandi98 – 1047
Turni111 – 1133
Helixi115 – 13117
Beta strandi135 – 1417
Helixi145 – 1484
Helixi149 – 16315
Beta strandi169 – 1724
Turni182 – 1854
Helixi186 – 20015
Beta strandi202 – 2043
Beta strandi206 – 2083
Helixi211 – 2144
Helixi217 – 2215
Beta strandi227 – 23711
Turni238 – 2403
Helixi243 – 25412
Beta strandi259 – 2679
Helixi277 – 28913
Beta strandi294 – 2996
Beta strandi302 – 3043
Helixi318 – 32811
Beta strandi367 – 3715
Beta strandi378 – 3858
Beta strandi389 – 3924
Beta strandi395 – 3984
Beta strandi401 – 4099
Beta strandi419 – 4246

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIWNMR-A367-426[»]
1EGZX-ray2.30A/B/C44-334[»]
ProteinModelPortaliP07103.
SMRiP07103. Positions 44-334, 366-426.

Miscellaneous databases

EvolutionaryTraceiP07103.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 332289Catalytic
Add
BLAST
Regioni333 – 36634Linker
Add
BLAST
Regioni367 – 42660Cellulose-binding
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000253566.
KOiK01179.
OMAiGGEKFYT.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMiSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07103-1 [UniParc]FASTAAdd to Basket

« Hide

MPLSYLDKNP VIDSKKHALR KKLFLSCAYF GLSLACLSSN AWASVEPLSV    50
NGNKIYAGEK AKSFAGNSLF WSNNGWGGEK FYTADTVASL KKDWKSSIVR 100
AAMGVQESGG YLQDPAGNKA KVERVVDAAI ANDMYAIIGW HSHSAENNRS 150
EAIRFFQEMA RKYGNKPNVI YEIYNEPLQV SWSNTIKPYA EAVISAIRAI 200
DPDNLIIVGT PSWSQNVDEA SRDPINAKNI AYTLHFYAGT HGESLRNKAR 250
QALNNGIALF VTEWGTVNAD GNGGVNQTET DAWVTFMRDN NISNANWALN 300
DKNEGASTYY PDSKNLTESG KKVKSIIQSW PYKAGSAASA TTDPSTDTTT 350
DTTVDEPTTT DTPATADCAN ANVYPNWVSK DWAGGQPTHN EAGQSIVYKG 400
NLYTANWYTA SVPGSDSSWT QVGSCN 426
Length:426
Mass (Da):46,418
Last modified:June 1, 1994 - v2
Checksum:iE78F2EE021FCA5DA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2953SNA → QLTQ in CAA68604. 1 Publication
Sequence conflicti350 – 36415TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604. 1 Publication
Add
BLAST
Sequence conflicti388 – 42639THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00540 Genomic DNA. Translation: CAA68604.1.
CP002038 Genomic DNA. Translation: ADM99099.1.
PIRiS03767.
RefSeqiYP_003883656.1. NC_014500.1.

Genome annotation databases

EnsemblBacteriaiADM99099; ADM99099; Dda3937_02793.
GeneIDi9734341.
KEGGiddd:Dda3937_02793.
PATRICi42318137. VBIDicDad25310_2889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00540 Genomic DNA. Translation: CAA68604.1 .
CP002038 Genomic DNA. Translation: ADM99099.1 .
PIRi S03767.
RefSeqi YP_003883656.1. NC_014500.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AIW NMR - A 367-426 [» ]
1EGZ X-ray 2.30 A/B/C 44-334 [» ]
ProteinModelPortali P07103.
SMRi P07103. Positions 44-334, 366-426.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADM99099 ; ADM99099 ; Dda3937_02793 .
GeneIDi 9734341.
KEGGi ddd:Dda3937_02793.
PATRICi 42318137. VBIDicDad25310_2889.

Phylogenomic databases

HOGENOMi HOG000253566.
KOi K01179.
OMAi GGEKFYT.

Enzyme and pathway databases

BioCyci DDAD198628:GHFQ-2956-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07103.

Family and domain databases

Gene3Di 2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00495. ChtBD3. 1 hit.
[Graphical view ]
SUPFAMi SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiGUNZ_DICD3
AccessioniPrimary (citable) accession number: P07103
Secondary accession number(s): E0SIP0
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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