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Q01786

- GUN5_THEFU

UniProt

Q01786 - GUN5_THEFU

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Protein

Endoglucanase E-5

Gene
celE
Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei299 – 2991Proton donor By similarity
Active sitei391 – 3911Nucleophile By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Add
BLAST
Chaini37 – 466430Endoglucanase E-5PRO_0000007866Add
BLAST

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi164 – 1685
Beta strandi172 – 1743
Beta strandi177 – 1793
Beta strandi189 – 1924
Helixi196 – 1994
Helixi200 – 2023
Helixi205 – 2139
Beta strandi218 – 22710
Helixi231 – 2333
Helixi235 – 25016
Turni251 – 2533
Beta strandi255 – 2617
Helixi268 – 2714
Helixi272 – 28615
Beta strandi290 – 2956
Helixi305 – 32218
Beta strandi328 – 3303
Helixi333 – 3364
Helixi340 – 3423
Helixi347 – 3515
Beta strandi357 – 36610
Turni367 – 3693
Helixi372 – 38413
Beta strandi387 – 3959
Helixi405 – 41814
Beta strandi422 – 4254
Beta strandi435 – 4373
Helixi441 – 4444
Helixi450 – 4523
Helixi455 – 46511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKRX-ray1.77A/B161-466[»]
2CKSX-ray1.60A/B161-466[»]
ProteinModelPortaliQ01786.
SMRiQ01786. Positions 161-466.

Miscellaneous databases

EvolutionaryTraceiQ01786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 139103CBM2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
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

MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD    50
NGYSASVTVR NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT 100
GVSWNSTIPP GGTASSGFIA SGSGEPTHCT INGAPCDEGS EPGGPGGPGT 150
PSPDPGTQPG TGTPVERYGK VQVCGTQLCD EHGNPVQLRG MSTHGIQWFD 200
HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD RMHQLIDMAT 250
ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP 300
NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA 350
ANPVNASNIM YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD 400
GANDFQMADR YIDLMAERKI GWTKWNYSDD FRSGAVFQPG TCASGGPWSG 450
SSLKASGQWV RSKLQS 466
Length:466
Mass (Da):49,801
Last modified:July 15, 1999 - v2
Checksum:i1CF0ADFBF2DEF82E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01577 Genomic DNA. Translation: AAC09379.1.
PIRiC42360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01577 Genomic DNA. Translation: AAC09379.1 .
PIRi C42360.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CKR X-ray 1.77 A/B 161-466 [» ]
2CKS X-ray 1.60 A/B 161-466 [» ]
ProteinModelPortali Q01786.
SMRi Q01786. Positions 161-466.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00696 .

Miscellaneous databases

EvolutionaryTracei Q01786.

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora fusca."
    Lao G., Ghangas G.S., Jung E.D., Wilson D.B.
    J. Bacteriol. 173:3397-3407(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: YX.
  2. Lao G., Ghangas G.S., Jung E.D., Wilson D.B.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects."
    Irwin D.C., Spezio M., Walker L.P., Wilson D.B.
    Biotechnol. Bioeng. 42:1002-1013(1993)
    Cited for: PROTEIN SEQUENCE OF 137-142 AND 157-166.
    Strain: YX.

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: December 11, 2013
This is version 87 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

External Data

Dasty 3

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