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P07986

- GUX_CELFI

UniProt

P07986 - GUX_CELFI

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Protein

Exoglucanase/xylanase

Gene

cex

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MPRTTPAPGH PARGARTALR TTRRRAATLV VGATVVLPAQ AATTLKEAAD
60 70 80 90 100
GAGRDFGFAL DPNRLSEAQY KAIADSEFNL VVAENAMKWD ATEPSQNSFS
110 120 130 140 150
FGAGDRVASY AADTGKELYG HTLVWHSQLP DWAKNLNGSA FESAMVNHVT
160 170 180 190 200
KVADHFEGKV ASWDVVNEAF ADGDGPPQDS AFQQKLGNGY IETAFRAARA
210 220 230 240 250
ADPTAKLCIN DYNVEGINAK SNSLYDLVKD FKARGVPLDC VGFQSHLIVG
260 270 280 290 300
QVPGDFRQNL QRFADLGVDV RITELDIRMR TPSDATKLAT QAADYKKVVQ
310 320 330 340 350
ACMQVTRCQG VTVWGITDKY SWVPDVFPGE GAALVWDASY AKKPAYAAVM
360 370 380 390 400
EAFGASPTPT PTTPTPTPTT PTPTPTSGPA GCQVLWGVNQ WNTGFTANVT
410 420 430 440 450
VKNTSSAPVD GWTLTFSFPS GQQVTQAWSS TVTQSGSAVT VRNAPWNGSI
460 470 480
PAGGTAQFGF NGSHTGTNAA PTAFSLNGTP CTVG
Length:484
Mass (Da):51,291
Last modified:August 1, 1988 - v1
Checksum:i6EE5486BC0E9B02F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15824 Genomic DNA. Translation: AAA56791.1.
PIRiA24994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15824 Genomic DNA. Translation: AAA56791.1 .
PIRi A24994.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 109 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