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P07986 (GUX_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exoglucanase/xylanase

Including the following 2 domains:

  1. Exoglucanase
    EC=3.2.1.91
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Beta-1,4-glycanase CEX
    Exocellobiohydrolase
  2. Endo-1,4-beta-xylanase B
    Short name=Xylanase B
    EC=3.2.1.8
Gene names
Name:cex
Synonyms:xynB
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 484443Exoglucanase/xylanase
PRO_0000007960

Regions

Domain375 – 484110CBM2
Region42 – 356315Catalytic
Region357 – 37620Linker ("hinge") (Pro-Thr box)

Sites

Active site1681Proton donor Ref.4
Active site2741Nucleophile Ref.2

Amino acid modifications

Disulfide bond208 ↔ 240 Ref.3
Disulfide bond302 ↔ 308 Ref.3
Disulfide bond382 ↔ 481 Ref.3

Experimental info

Mutagenesis1681E → A, D or G: Reduced activity. Ref.9

Secondary structure

1 ................................................................................ 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07986 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 6EE5486BC0E9B02F

FASTA48451,291
        10         20         30         40         50         60 
MPRTTPAPGH PARGARTALR TTRRRAATLV VGATVVLPAQ AATTLKEAAD GAGRDFGFAL 

        70         80         90        100        110        120 
DPNRLSEAQY KAIADSEFNL VVAENAMKWD ATEPSQNSFS FGAGDRVASY AADTGKELYG 

       130        140        150        160        170        180 
HTLVWHSQLP DWAKNLNGSA FESAMVNHVT KVADHFEGKV ASWDVVNEAF ADGDGPPQDS 

       190        200        210        220        230        240 
AFQQKLGNGY IETAFRAARA ADPTAKLCIN DYNVEGINAK SNSLYDLVKD FKARGVPLDC 

       250        260        270        280        290        300 
VGFQSHLIVG QVPGDFRQNL QRFADLGVDV RITELDIRMR TPSDATKLAT QAADYKKVVQ 

       310        320        330        340        350        360 
ACMQVTRCQG VTVWGITDKY SWVPDVFPGE GAALVWDASY AKKPAYAAVM EAFGASPTPT 

       370        380        390        400        410        420 
PTTPTPTPTT PTPTPTSGPA GCQVLWGVNQ WNTGFTANVT VKNTSSAPVD GWTLTFSFPS 

       430        440        450        460        470        480 
GQQVTQAWSS TVTQSGSAVT VRNAPWNGSI PAGGTAQFGF NGSHTGTNAA PTAFSLNGTP 


CTVG

« Hide

References

[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]"Structural and functional relationships in two families of beta-1,4-glycanases."
Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
Eur. J. Biochem. 202:367-377(1991) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M15824 Genomic DNA. Translation: AAA56791.1.
PIRA24994.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.00A43-353[»]
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[»]
ProteinModelPortalP07986.
SMRP07986. Positions 42-353, 376-484.
ModBaseSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. 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]
PfamPF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49384. Cellul_bind. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07986.

Entry information

Entry nameGUX_CELFI
AccessionPrimary (citable) accession number: P07986
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents