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Protein

Endoglucanase Z

Gene

celZ

Organism
Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei176Proton donor1
Active sitei263NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya
Proteomesi
  • UP000006859 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi141H → A: Loss of activity. 1 Publication1
Mutagenesisi176E → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 43Add BLAST43
ChainiPRO_000000786044 – 426Endoglucanase ZAdd BLAST383

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi368 ↔ 4251 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi198628.Dda3937_02793.

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 51Combined sources4
Beta strandi54 – 57Combined sources4
Beta strandi65 – 71Combined sources7
Helixi78 – 81Combined sources4
Helixi84 – 92Combined sources9
Beta strandi98 – 104Combined sources7
Turni111 – 113Combined sources3
Helixi115 – 131Combined sources17
Beta strandi135 – 141Combined sources7
Helixi145 – 148Combined sources4
Helixi149 – 163Combined sources15
Beta strandi169 – 172Combined sources4
Turni182 – 185Combined sources4
Helixi186 – 200Combined sources15
Beta strandi202 – 204Combined sources3
Beta strandi206 – 208Combined sources3
Helixi211 – 214Combined sources4
Helixi217 – 221Combined sources5
Beta strandi227 – 237Combined sources11
Turni238 – 240Combined sources3
Helixi243 – 254Combined sources12
Beta strandi259 – 267Combined sources9
Helixi277 – 289Combined sources13
Beta strandi294 – 299Combined sources6
Beta strandi302 – 304Combined sources3
Helixi318 – 328Combined sources11
Beta strandi367 – 371Combined sources5
Beta strandi378 – 385Combined sources8
Beta strandi389 – 392Combined sources4
Beta strandi395 – 398Combined sources4
Beta strandi401 – 409Combined sources9
Beta strandi419 – 424Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIWNMR-A367-426[»]
1EGZX-ray2.30A/B/C44-334[»]
ProteinModelPortaliP07103.
SMRiP07103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07103.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 332CatalyticAdd BLAST289
Regioni333 – 366LinkerAdd BLAST34
Regioni367 – 426Cellulose-bindingAdd BLAST60

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000253566.
KOiK01179.
OMAiSHSAENN.
OrthoDBiPOG091H0FFG.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR032798. CBM_5_12_2.
IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF14600. CBM_5_12_2. 1 hit.
PF00150. 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)DescriptionActionsGraphical viewLength
Sequence conflicti293 – 295SNA → QLTQ in CAA68604 (PubMed:2835589).Curated3
Sequence conflicti350 – 364TDTTV…TDTPA → MTPPLTNRPQPTHRQ in CAA68604 (PubMed:2835589).CuratedAdd BLAST15
Sequence conflicti388 – 426THNEA…VGSCN → LITKQANRSSTKATCIPQTG TPHPFRAAIPPGRRLVAVTN (PubMed:2835589).CuratedAdd BLAST39

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00540 Genomic DNA. Translation: CAA68604.1.
CP002038 Genomic DNA. Translation: ADM99099.1.
PIRiS03767.
RefSeqiWP_013318538.1. 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.
PIRiS03767.
RefSeqiWP_013318538.1. NC_014500.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIWNMR-A367-426[»]
1EGZX-ray2.30A/B/C44-334[»]
ProteinModelPortaliP07103.
SMRiP07103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198628.Dda3937_02793.

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADM99099; ADM99099; Dda3937_02793.
GeneIDi9734341.
KEGGiddd:Dda3937_02793.
PATRICi42318137. VBIDicDad25310_2889.

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000253566.
KOiK01179.
OMAiSHSAENN.
OrthoDBiPOG091H0FFG.

Miscellaneous databases

EvolutionaryTraceiP07103.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR032798. CBM_5_12_2.
IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF14600. CBM_5_12_2. 1 hit.
PF00150. 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]
ProtoNetiSearch...

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 2, 2016
This is version 126 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.