P07103 (GUNZ_DICD3) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya › Dickeya dadantii

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 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

43

Chain

44 – 426

383

Endoglucanase Z

PRO_0000007860

Regions

Region

44 – 332

289

Catalytic

Region

333 – 366

34

Linker

Region

367 – 426

60

Cellulose-binding

Sites

Active site

176

1

Proton donor

Active site

263

1

Nucleophile By similarity

Amino acid modifications

Disulfide bond

368 ↔ 425

Ref.2

Experimental info

Mutagenesis

141

1

H → A: Loss of activity.

Mutagenesis

176

1

E → A: Loss of activity.

Sequence conflict

293 – 295

3

SNA → QLTQ in CAA68604. Ref.1

Sequence conflict

350 – 364

15

TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604. Ref.1

Sequence conflict

388 – 426

39

THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN Ref.1

Secondary structure

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426

Helix Strand Turn

Details...

Beta strand

48 – 51

4

Beta strand

54 – 57

4

Beta strand

65 – 71

7

Helix

78 – 81

4

Helix

84 – 92

9

Beta strand

98 – 104

7

Turn

111 – 113

3

Helix

115 – 131

17

Beta strand

135 – 141

7

Helix

145 – 148

4

Helix

149 – 163

15

Beta strand

169 – 172

4

Turn

182 – 185

4

Helix

186 – 200

15

Beta strand

202 – 204

3

Beta strand

206 – 208

3

Helix

211 – 214

4

Helix

217 – 221

5

Beta strand

227 – 237

11

Turn

238 – 240

3

Helix

243 – 254

12

Beta strand

259 – 267

9

Helix

277 – 289

13

Beta strand

294 – 299

6

Beta strand

302 – 304

3

Helix

318 – 328

11

Beta strand

367 – 371

5

Beta strand

378 – 385

8

Beta strand

389 – 392

4

Beta strand

395 – 398

4

Beta strand

401 – 409

9

Beta strand

419 – 424

6

Sequences

	Sequence		Length	Mass (Da)
	P07103 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: E78F2EE021FCA5DA	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

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] [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. , 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.

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

EnsemblBacteria

ADM99099; ADM99099; Dda3937_02793.

GeneID

9734341.

KEGG

ddd:Dda3937_02793.

PATRIC

42318137. VBIDicDad25310_2889.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HOG000253566.

KO

K01179.

OMA

SHSAENN.

Enzyme and pathway databases

BioCyc

DDAD198628:GHFQ-2955-MONOMER.

Family and domain databases

Gene3D

2.10.10.20. 1 hit.
3.20.20.80. 1 hit.

InterPro

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

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...

Other

EvolutionaryTrace

P07103.

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:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program