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P07986

- GUX_CELFI

UniProt

P07986 - GUX_CELFI

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Protein
Exoglucanase/xylanase
Gene
cex, xynB
Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication

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
Complete GO annotation...

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 – 4141
Add
BLAST
Chaini42 – 484443Exoglucanase/xylanase
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP07986.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini375 – 484110CBM2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 356315Catalytic
Add
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

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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: July 9, 2014
This is version 107 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

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