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Protein

Endoglucanase 5

Gene

celV

Organism
Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endoglucanase with some exoglucanase activity.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

pH dependencei

Optimum pH is about 7.0.

Temperature dependencei

Optimum temperature is about 42 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei168Proton donorBy similarity1
Active sitei256NucleophileBy 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

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 5 (EC:3.2.1.4)
Alternative name(s):
Cellulase V
Endo-1,4-beta-glucanase V
Endoglucanase V
Gene namesi
Name:celV
OrganismiPectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)
Taxonomic identifieri555 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaePectobacterium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000000785832 – 505Endoglucanase 5Add BLAST474

Interactioni

Protein-protein interaction databases

STRINGi561230.PC1_2337.

Structurei

3D structure databases

ProteinModelPortaliQ47096.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini353 – 505CBM3PROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 334CatalyticAdd BLAST303
Regioni335 – 352LinkerAdd BLAST18

Sequence similaritiesi

Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.

Family and domain databases

Gene3Di2.60.40.710. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q47096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD
60 70 80 90 100
EQGKRVQLRG ISSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG
110 120 130 140 150
YISNPSLANK VKEAVAAAQS LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE
160 170 180 190 200
MAGLYGSSPN VIYEIANEPN GGVTWNGQIR PYALEVTDTI RSKDPDNLII
210 220 230 240 250
VGTGTWSQDI HDAADNQLPD PNTMYALHFY AGTHGQFLRD RIDYAQSRGA
260 270 280 290 300
AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA
310 320 330 340 350
ALAPGASKSG GWTEQNLSTS GKFVREQIRA GANLGGGDTP TTPTEPTNPG
360 370 380 390 400
NGTTGDVVLQ YRNVDNNPSD DAIRMAVNIK NTGSTPIKLS DLQVRYYFHD
410 420 430 440 450
DGKPGANLFV DWANVGPNNI VTSTGTPAAS TDKANRYVLV TFSSGAGSLQ
460 470 480 490 500
PGAETGEVQV RIHAGDWSNV NETNDYSYGA NVTSYANWDK ITVHDKGTLV

WGVEP
Length:505
Mass (Da):54,900
Last modified:November 1, 1996 - v1
Checksum:iDBEA9337BB4D2623
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76000 Genomic DNA. Translation: CAA53592.1.
PIRiS39962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76000 Genomic DNA. Translation: CAA53592.1.
PIRiS39962.

3D structure databases

ProteinModelPortaliQ47096.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi561230.PC1_2337.

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.

Family and domain databases

Gene3Di2.60.40.710. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUNV_PECCC
AccessioniPrimary (citable) accession number: Q47096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.