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P07986

- GUX_CELFI

UniProt

P07986 - GUX_CELFI

Protein

Exoglucanase/xylanase

Gene

cex

Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity.
    The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

    Catalytic activityi

    Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681Proton donor1 Publication
    Active sitei274 – 2741Nucleophile1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
    2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
    3. polysaccharide binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW
    2. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation, Xylan degradation

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    GH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase/xylanase
    Including the following 2 domains:
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Beta-1,4-glycanase CEX
    Exocellobiohydrolase
    Endo-1,4-beta-xylanase B (EC:3.2.1.8)
    Short name:
    Xylanase B
    Gene namesi
    Name:cex
    Synonyms:xynB
    OrganismiCellulomonas fimi
    Taxonomic identifieri1708 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681E → A, D or G: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Add
    BLAST
    Chaini42 – 484443Exoglucanase/xylanasePRO_0000007960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi208 ↔ 2401 Publication
    Disulfide bondi302 ↔ 3081 Publication
    Disulfide bondi382 ↔ 4811 Publication

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 528
    Beta strandi55 – 606
    Helixi62 – 665
    Helixi68 – 7710
    Beta strandi79 – 857
    Helixi89 – 924
    Helixi102 – 11413
    Beta strandi117 – 12812
    Helixi131 – 1344
    Helixi138 – 15619
    Turni157 – 1593
    Beta strandi162 – 1676
    Beta strandi174 – 1763
    Helixi181 – 1866
    Helixi187 – 1893
    Helixi190 – 20112
    Beta strandi203 – 21311
    Beta strandi215 – 2184
    Helixi219 – 23416
    Beta strandi240 – 2434
    Beta strandi246 – 2483
    Helixi256 – 2649
    Turni265 – 2673
    Beta strandi269 – 28214
    Helixi285 – 30319
    Beta strandi308 – 3147
    Turni318 – 3203
    Helixi323 – 3264
    Beta strandi334 – 3363
    Helixi344 – 35310
    Beta strandi382 – 3854
    Beta strandi388 – 40316
    Beta strandi405 – 4073
    Beta strandi409 – 4179
    Beta strandi419 – 4213
    Beta strandi423 – 43513
    Beta strandi438 – 4436
    Helixi446 – 4483
    Beta strandi452 – 46312
    Beta strandi465 – 4673
    Beta strandi474 – 4763
    Beta strandi479 – 4835

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EXGNMR-A377-484[»]
    1EXHNMR-A377-484[»]
    1EXPX-ray1.80A42-353[»]
    1FH7X-ray1.82A42-353[»]
    1FH8X-ray1.95A42-353[»]
    1FH9X-ray1.72A42-353[»]
    1FHDX-ray1.90A42-353[»]
    1J01X-ray2.00A42-353[»]
    2EXOX-ray1.80A42-353[»]
    2HISX-ray1.84A42-353[»]
    2XYLX-ray1.90A42-353[»]
    3CUFX-ray1.67A42-356[»]
    3CUGX-ray1.68A42-356[»]
    3CUHX-ray1.89A42-356[»]
    3CUIX-ray1.50A42-356[»]
    3CUJX-ray1.70A42-356[»]
    ProteinModelPortaliP07986.
    SMRiP07986. Positions 42-353, 376-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07986.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini375 – 484110CBM2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 356315CatalyticAdd
    BLAST
    Regioni357 – 37620Linker ("hinge") (Pro-Thr box)Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, 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.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00637. CBD_II. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07986-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRTTPAPGH PARGARTALR TTRRRAATLV VGATVVLPAQ AATTLKEAAD    50
    GAGRDFGFAL DPNRLSEAQY KAIADSEFNL VVAENAMKWD ATEPSQNSFS 100
    FGAGDRVASY AADTGKELYG HTLVWHSQLP DWAKNLNGSA FESAMVNHVT 150
    KVADHFEGKV ASWDVVNEAF ADGDGPPQDS AFQQKLGNGY IETAFRAARA 200
    ADPTAKLCIN DYNVEGINAK SNSLYDLVKD FKARGVPLDC VGFQSHLIVG 250
    QVPGDFRQNL QRFADLGVDV RITELDIRMR TPSDATKLAT QAADYKKVVQ 300
    ACMQVTRCQG VTVWGITDKY SWVPDVFPGE GAALVWDASY AKKPAYAAVM 350
    EAFGASPTPT PTTPTPTPTT PTPTPTSGPA GCQVLWGVNQ WNTGFTANVT 400
    VKNTSSAPVD GWTLTFSFPS GQQVTQAWSS TVTQSGSAVT VRNAPWNGSI 450
    PAGGTAQFGF NGSHTGTNAA PTAFSLNGTP CTVG 484
    Length:484
    Mass (Da):51,291
    Last modified:August 1, 1988 - v1
    Checksum:i6EE5486BC0E9B02F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15824 Genomic DNA. Translation: AAA56791.1.
    PIRiA24994.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15824 Genomic DNA. Translation: AAA56791.1 .
    PIRi A24994.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EXG NMR - A 377-484 [» ]
    1EXH NMR - A 377-484 [» ]
    1EXP X-ray 1.80 A 42-353 [» ]
    1FH7 X-ray 1.82 A 42-353 [» ]
    1FH8 X-ray 1.95 A 42-353 [» ]
    1FH9 X-ray 1.72 A 42-353 [» ]
    1FHD X-ray 1.90 A 42-353 [» ]
    1J01 X-ray 2.00 A 42-353 [» ]
    2EXO X-ray 1.80 A 42-353 [» ]
    2HIS X-ray 1.84 A 42-353 [» ]
    2XYL X-ray 1.90 A 42-353 [» ]
    3CUF X-ray 1.67 A 42-356 [» ]
    3CUG X-ray 1.68 A 42-356 [» ]
    3CUH X-ray 1.89 A 42-356 [» ]
    3CUI X-ray 1.50 A 42-356 [» ]
    3CUJ X-ray 1.70 A 42-356 [» ]
    ProteinModelPortali P07986.
    SMRi P07986. Positions 42-353, 376-484.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P07986.

    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.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00637. CBD_II. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the gene encoding the exoglucanase of Cellulomonas fimi."
      O'Neill G., Goh S.H., Warren R.A.J., Kilburn D.G., Miller R.C. Jr.
      Gene 44:325-330(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Glutamic acid 274 is the nucleophile in the active site of a 'retaining' exoglucanase from Cellulomonas fimi."
      Tull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J., Aebersold R.
      J. Biol. Chem. 266:15621-15625(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE GLU-274.
    3. Cited for: DISULFIDE BONDS.
    4. "Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi."
      White A., Withers S.G., Gilkes N.R., Rose D.R.
      Biochemistry 33:12546-12552(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    5. "Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase."
      White A., Tull D., Johns K., Withers S.G., Rose D.R.
      Nat. Struct. Biol. 3:149-154(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    6. "Exploring the cellulose/xylan specificity of the beta-1,4-glycanase cex from Cellulomonas fimi through crystallography and mutation."
      Notenboom V., Birsan C., Warren R.A.J., Withers S.G., Rose D.R.
      Biochemistry 37:4751-4758(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-353.
    7. "Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants."
      Notenboom V., Birsan C., Nitz M., Rose D.R., Warren R.A., Withers S.G.
      Nat. Struct. Biol. 5:812-818(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 42-353.
      Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
    8. "Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy."
      Xu G.-Y., Ong E., Gilkes N.R., Kilburn D.G., Muhandiram D.R., Harris-Brandts M., Carver J.P., Kay L.E., Harvey T.S.
      Biochemistry 34:6993-7009(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 377-484.
    9. "The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants."
      Macleod A.M., Lindhorst T., Withers S.G., Warren R.A.J.
      Biochemistry 33:6371-6376(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-168.
    10. "Detailed structural analysis of glycosidase/inhibitor interactions: complexes of Cex from Cellulomonas fimi with xylobiose-derived aza-sugars."
      Notenboom V., Williams S.J., Hoos R., Withers S.G., Rose D.R.
      Biochemistry 39:11553-11563(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 43-354.

    Entry informationi

    Entry nameiGUX_CELFI
    AccessioniPrimary (citable) accession number: P07986
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The linker region (also termed "hinge") may be a potential site for proteolysis.

    Keywords - Technical termi

    3D-structure, Multifunctional enzyme

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3