Endoglucanase Z precursor - Dickeya dadantii (strain 3937)

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P07103 (GUNZ_DICD3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) [Complete proteome] [HAMAP]

Taxonomic identifier

198628 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 43

Chain

44 – 426

383

Endoglucanase Z

PRO_0000007860

Regions

Region

44 – 332

289

Catalytic

Region

333 – 366

Linker

Region

367 – 426

Cellulose-binding

Sites

Active site

176

Proton donor

Active site

263

Nucleophile By similarity

Amino acid modifications

Disulfide bond

368 ↔ 425

Ref.2

Experimental info

Mutagenesis

141

H → A: Loss of activity.

Mutagenesis

176

E → A: Loss of activity.

Sequence conflict

293 – 295

SNA → QLTQ in CAA68604. Ref.1

Sequence conflict

350 – 364

TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604. Ref.1

Sequence conflict

388 – 426

THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN Ref.1

Secondary structure

426

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07103 [UniParc].

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

FASTA

426

46,418

        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' referencesShow '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: 2835589] [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: 8152378] [Abstract] Cited for: SEQUENCE REVISION, DISULFIDE BOND.
[3]	"Complete genome sequence of Dickeya dadantii 3937." International Erwinia Consortium Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases 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: 1677466] [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: 1563515] [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: 9405041] [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: 11501995] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 44-335.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00540 Genomic DNA. Translation: CAA68604.1.
CP002038 Genomic DNA. Translation: ADM99099.1.

PIR

S03767.

RefSeq

YP_003883656.1. NC_014500.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AIW	NMR	-	A	367-426	[»]
1EGZ	X-ray	2.30	A/B/C	44-334	[»]

ProteinModelPortal

P07103.

SMR

P07103. Positions 44-334, 366-426.

ModBase

Search...

Protein family/group databases

CAZy

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

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

9734341.

GenomeReviews

Gene locus Dda3937_02793 in contig CP002038_GR.

KEGG

ddd:Dda3937_02793.

PATRIC

42318137. VBIDicDad25310_2889.

Organism-specific databases

CMR

Search...

Family and domain databases

InterPro

IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.10.10.20. G3DSA:2.10.10.20. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

K01179.

Pfam

PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM00495. ChtBD3. 1 hit.
[Graphical view]

SUPFAM

SSF51055. CBM_5_12. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUNZ_DICD3

Accession

Primary (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:	January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Family and domain databases

Entry information

Relevant documents