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Protein

Endoglucanase E-5

Gene

celE

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei299Proton donorBy similarity1
Active sitei391NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E-5 (EC:3.2.1.4)
Alternative name(s):
Cellulase E-5
Cellulase E5
Endo-1,4-beta-glucanase E-4
Gene namesi
Name:celE
OrganismiThermobifida fusca (Thermomonospora fusca)
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Add BLAST36
ChainiPRO_000000786637 – 466Endoglucanase E-5Add BLAST430

Interactioni

Protein-protein interaction databases

STRINGi269800.Tfu_0901.

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi164 – 168Combined sources5
Beta strandi172 – 174Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi189 – 192Combined sources4
Helixi196 – 199Combined sources4
Helixi200 – 202Combined sources3
Helixi205 – 213Combined sources9
Beta strandi218 – 227Combined sources10
Helixi231 – 233Combined sources3
Helixi235 – 250Combined sources16
Turni251 – 253Combined sources3
Beta strandi255 – 261Combined sources7
Helixi268 – 271Combined sources4
Helixi272 – 286Combined sources15
Beta strandi290 – 295Combined sources6
Helixi305 – 322Combined sources18
Beta strandi328 – 330Combined sources3
Helixi333 – 336Combined sources4
Helixi340 – 342Combined sources3
Helixi347 – 351Combined sources5
Beta strandi357 – 366Combined sources10
Turni367 – 369Combined sources3
Helixi372 – 384Combined sources13
Beta strandi387 – 395Combined sources9
Helixi405 – 418Combined sources14
Beta strandi422 – 425Combined sources4
Beta strandi435 – 437Combined sources3
Helixi441 – 444Combined sources4
Helixi450 – 452Combined sources3
Helixi455 – 465Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKRX-ray1.77A/B161-466[»]
2CKSX-ray1.60A/B161-466[»]
ProteinModelPortaliQ01786.
SMRiQ01786.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 139CBM2PROSITE-ProRule annotationAdd BLAST103

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107SMB. Bacteria.
COG2730. LUCA.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 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.

Q01786-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD
60 70 80 90 100
NGYSASVTVR NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT
110 120 130 140 150
GVSWNSTIPP GGTASSGFIA SGSGEPTHCT INGAPCDEGS EPGGPGGPGT
160 170 180 190 200
PSPDPGTQPG TGTPVERYGK VQVCGTQLCD EHGNPVQLRG MSTHGIQWFD
210 220 230 240 250
HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD RMHQLIDMAT
260 270 280 290 300
ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP
310 320 330 340 350
NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA
360 370 380 390 400
ANPVNASNIM YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD
410 420 430 440 450
GANDFQMADR YIDLMAERKI GWTKWNYSDD FRSGAVFQPG TCASGGPWSG
460
SSLKASGQWV RSKLQS
Length:466
Mass (Da):49,801
Last modified:July 15, 1999 - v2
Checksum:i1CF0ADFBF2DEF82E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01577 Genomic DNA. Translation: AAC09379.1.
PIRiC42360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01577 Genomic DNA. Translation: AAC09379.1.
PIRiC42360.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKRX-ray1.77A/B161-466[»]
2CKSX-ray1.60A/B161-466[»]
ProteinModelPortaliQ01786.
SMRiQ01786.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_0901.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107SMB. Bacteria.
COG2730. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00696.

Miscellaneous databases

EvolutionaryTraceiQ01786.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN5_THEFU
AccessioniPrimary (citable) accession number: Q01786
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1999
Last modified: November 2, 2016
This is version 96 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, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.