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P26222

- GUN2_THEFU

UniProt

P26222 - GUN2_THEFU

Protein

Endoglucanase E-2

Gene

celB

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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

    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 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Chaini32 – 441410Endoglucanase E-2PRO_0000007909Add
    BLAST

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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: October 1, 2014
    This is version 111 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