Reviewed, UniProtKB/Swiss-Prot P07103 (GUNZ_DICD3)

Names and origin

Protein names

Recommended name:
    Endoglucanase Z
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase Z
      Short name=EGZ
    Cellulase Z

Gene names

Name:	celZ
Synonyms:	cel5

Organism

Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))

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
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

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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

426

Helix Strand Turn

Details...

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)
	P07103-1 [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

[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].
[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]	"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.
[4]	"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.
[5]	"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.
[6]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00540 Genomic DNA. Translation: CAA68604.1.

PIR

S03767.

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein family/group databases

CAZy

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

Family and domain databases

InterPro

IPR003610. CBM_5_12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF02839. CBM_5_12. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM00495. ChtBD3. 1 hit.
[Graphical view]

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUNZ_DICD3

Accession

Primary (citable) accession number: P07103

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)