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P07103

- GUNZ_DICD3

UniProt

P07103 - GUNZ_DICD3

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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

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
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-KW
Complete GO annotation...

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 – 514Combined sources
Beta strandi54 – 574Combined sources
Beta strandi65 – 717Combined sources
Helixi78 – 814Combined sources
Helixi84 – 929Combined sources
Beta strandi98 – 1047Combined sources
Turni111 – 1133Combined sources
Helixi115 – 13117Combined sources
Beta strandi135 – 1417Combined sources
Helixi145 – 1484Combined sources
Helixi149 – 16315Combined sources
Beta strandi169 – 1724Combined sources
Turni182 – 1854Combined sources
Helixi186 – 20015Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi206 – 2083Combined sources
Helixi211 – 2144Combined sources
Helixi217 – 2215Combined sources
Beta strandi227 – 23711Combined sources
Turni238 – 2403Combined sources
Helixi243 – 25412Combined sources
Beta strandi259 – 2679Combined sources
Helixi277 – 28913Combined sources
Beta strandi294 – 2996Combined sources
Beta strandi302 – 3043Combined sources
Helixi318 – 32811Combined sources
Beta strandi367 – 3715Combined sources
Beta strandi378 – 3858Combined sources
Beta strandi389 – 3924Combined sources
Beta strandi395 – 3984Combined sources
Beta strandi401 – 4099Combined sources
Beta strandi419 – 4246Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MPLSYLDKNP VIDSKKHALR KKLFLSCAYF GLSLACLSSN AWASVEPLSV
60 70 80 90 100
NGNKIYAGEK AKSFAGNSLF WSNNGWGGEK FYTADTVASL KKDWKSSIVR
110 120 130 140 150
AAMGVQESGG YLQDPAGNKA KVERVVDAAI ANDMYAIIGW HSHSAENNRS
160 170 180 190 200
EAIRFFQEMA RKYGNKPNVI YEIYNEPLQV SWSNTIKPYA EAVISAIRAI
210 220 230 240 250
DPDNLIIVGT PSWSQNVDEA SRDPINAKNI AYTLHFYAGT HGESLRNKAR
260 270 280 290 300
QALNNGIALF VTEWGTVNAD GNGGVNQTET DAWVTFMRDN NISNANWALN
310 320 330 340 350
DKNEGASTYY PDSKNLTESG KKVKSIIQSW PYKAGSAASA TTDPSTDTTT
360 370 380 390 400
DTTVDEPTTT DTPATADCAN ANVYPNWVSK DWAGGQPTHN EAGQSIVYKG
410 420
NLYTANWYTA SVPGSDSSWT QVGSCN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 114 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