Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01786

- GUN5_THEFU

UniProt

Q01786 - GUN5_THEFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 donorBy similarity
Active sitei391 – 3911NucleophileBy 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 – 1685Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi189 – 1924Combined sources
Helixi196 – 1994Combined sources
Helixi200 – 2023Combined sources
Helixi205 – 2139Combined sources
Beta strandi218 – 22710Combined sources
Helixi231 – 2333Combined sources
Helixi235 – 25016Combined sources
Turni251 – 2533Combined sources
Beta strandi255 – 2617Combined sources
Helixi268 – 2714Combined sources
Helixi272 – 28615Combined sources
Beta strandi290 – 2956Combined sources
Helixi305 – 32218Combined sources
Beta strandi328 – 3303Combined sources
Helixi333 – 3364Combined sources
Helixi340 – 3423Combined sources
Helixi347 – 3515Combined sources
Beta strandi357 – 36610Combined sources
Turni367 – 3693Combined sources
Helixi372 – 38413Combined sources
Beta strandi387 – 3959Combined sources
Helixi405 – 41814Combined sources
Beta strandi422 – 4254Combined sources
Beta strandi435 – 4373Combined sources
Helixi441 – 4444Combined sources
Helixi450 – 4523Combined sources
Helixi455 – 46511Combined sources

3D structure databases

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

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

        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 .
PIRi C42360.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 89 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