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P26222

- GUN2_THEFU

UniProt

P26222 - GUN2_THEFU

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Protein

Endoglucanase E-2

Gene
celB
Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed - Annotation score: 5 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 sitei110 – 1101
Active sitei148 – 1481Proton donor
Active sitei296 – 2961Nucleophile

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.
GH6. Glycoside Hydrolase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E-2 (EC:3.2.1.4)
Alternative name(s):
Cellulase E-2
Cellulase E2
Endo-1,4-beta-glucanase E-2
Gene namesi
Name:celB
OrganismiThermobifida fusca (Thermomonospora fusca)
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1631E → G: Loss of ability to form dimers. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Tat-type signal1 PublicationAdd
BLAST
Chaini32 – 441410Endoglucanase E-2PRO_0000007909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 156
Disulfide bondi263 ↔ 298
Disulfide bondi346 ↔ 438 Reviewed prediction

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363
Helixi43 – 508
Helixi57 – 637
Turni64 – 663
Beta strandi71 – 733
Turni78 – 803
Helixi81 – 9515
Beta strandi100 – 1034
Beta strandi107 – 1093
Beta strandi116 – 1183
Beta strandi119 – 1213
Helixi122 – 13413
Turni135 – 1384
Beta strandi142 – 1454
Helixi149 – 1535
Helixi158 – 17821
Beta strandi183 – 1875
Beta strandi191 – 1944
Helixi196 – 20510
Helixi208 – 2114
Beta strandi213 – 2186
Helixi225 – 23915
Beta strandi245 – 2495
Beta strandi274 – 2763
Beta strandi283 – 2886
Beta strandi297 – 3015
Helixi307 – 3159

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMLX-ray1.80A32-317[»]
2BODX-ray1.50X32-317[»]
2BOEX-ray1.15X32-317[»]
2BOFX-ray1.64X32-317[»]
2BOGX-ray1.04X32-317[»]
3RPTX-ray1.30A/X33-317[»]
ProteinModelPortaliP26222.
SMRiP26222. Positions 32-317.

Miscellaneous databases

EvolutionaryTraceiP26222.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini339 – 441103CBM2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 320289CatalyticAdd
BLAST
Regioni321 – 34020LinkerAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK01179.
OrthoDBiEOG6P06X3.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26222-1 [UniParc]FASTAAdd to Basket

« Hide

MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN    50
NPNDPRTPVI RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI 100
LVVYNAPGRD CGNHSSGGAP SHSAYRSWID EFAAGLKNRP AYIIVEPDLI 150
SLMSSCMQHV QQEVLETMAY AGKALKAGSS QARIYFDAGH SAWHSPAQMA 200
SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG NPSLRAVIDT 250
SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA 300
GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY 350
TIANEWNDGF QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS 400
SVTARNVGHN GTLSQGASTE FGFVGSKGNS NSVPTLTCAA S 441
Length:441
Mass (Da):45,844
Last modified:February 1, 1996 - v2
Checksum:i87218E4537092AE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73321 mRNA. Translation: AAC06388.1.
PIRiA42360.
T12011.
RefSeqiYP_289135.1. NC_007333.1.

Genome annotation databases

GeneIDi3580066.
KEGGitfu:Tfu_1074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73321 mRNA. Translation: AAC06388.1 .
PIRi A42360.
T12011.
RefSeqi YP_289135.1. NC_007333.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TML X-ray 1.80 A 32-317 [» ]
2BOD X-ray 1.50 X 32-317 [» ]
2BOE X-ray 1.15 X 32-317 [» ]
2BOF X-ray 1.64 X 32-317 [» ]
2BOG X-ray 1.04 X 32-317 [» ]
3RPT X-ray 1.30 A/X 33-317 [» ]
ProteinModelPortali P26222.
SMRi P26222. Positions 32-317.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3580066.
KEGGi tfu:Tfu_1074.

Phylogenomic databases

KOi K01179.
OrthoDBi EOG6P06X3.

Enzyme and pathway databases

UniPathwayi UPA00696 .

Miscellaneous databases

EvolutionaryTracei P26222.

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProi IPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PRINTSi PR00733. GLHYDRLASE6.
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 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. Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B.
    Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    Strain: YX.
  3. "Cellulases of Thermomonospora fusca."
    Wilson D.B.
    Methods Enzymol. 160:314-323(1988)
    Cited for: PROTEIN SEQUENCE OF 32-47.
  4. "Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2."
    McGinnis K., Kroupis C., Wilson D.B.
    Biochemistry 32:8146-8150(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF GLU-163.
  5. "Crystal structure of the catalytic domain of a thermophilic endocellulase."
    Spezio M., Wilson D.B., Karplus P.A.
    Biochemistry 32:9906-9916(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317.

Entry informationi

Entry nameiGUN2_THEFU
AccessioniPrimary (citable) accession number: P26222
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: December 11, 2013
This is version 110 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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