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P07103

- GUNZ_DICD3

UniProt

P07103 - GUNZ_DICD3

Protein

Endoglucanase Z

Gene

celZ

Organism
Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    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 – 2631NucleophileBy 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

    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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi141 – 1411H → A: Loss of activity. 1 Publication
    Mutagenesisi176 – 1761E → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4343Add
    BLAST
    Chaini44 – 426383Endoglucanase ZPRO_0000007860Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    426
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07103.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 332289CatalyticAdd
    BLAST
    Regioni333 – 36634LinkerAdd
    BLAST
    Regioni367 – 42660Cellulose-bindingAdd
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti293 – 2953SNA → QLTQ in CAA68604. (PubMed:2835589)Curated
    Sequence conflicti350 – 36415TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604. (PubMed:2835589)CuratedAdd
    BLAST
    Sequence conflicti388 – 42639THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN(PubMed:2835589)CuratedAdd
    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

    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: October 1, 2014
    This is version 112 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, Reference 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