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Protein

Exoglucanase/xylanase

Gene

cex

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: 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 disaccharide 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)DescriptionActionsGraphical viewLength
Active sitei168Proton donor1 Publication1
Active sitei274NucleophilePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi168E → A, D or G: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 41Add BLAST41
ChainiPRO_000000796042 – 484Exoglucanase/xylanaseAdd BLAST443

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi208 ↔ 2401 Publication
Disulfide bondi302 ↔ 3081 Publication
Disulfide bondi382 ↔ 4811 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP07986.

Interactioni

Protein-protein interaction databases

STRINGi590998.Celf_1271.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 52Combined sources8
Beta strandi55 – 60Combined sources6
Helixi62 – 66Combined sources5
Helixi68 – 77Combined sources10
Beta strandi79 – 85Combined sources7
Helixi89 – 92Combined sources4
Helixi102 – 114Combined sources13
Beta strandi117 – 128Combined sources12
Helixi131 – 134Combined sources4
Helixi138 – 156Combined sources19
Turni157 – 159Combined sources3
Beta strandi162 – 167Combined sources6
Beta strandi174 – 176Combined sources3
Helixi181 – 186Combined sources6
Helixi187 – 189Combined sources3
Helixi190 – 201Combined sources12
Beta strandi203 – 213Combined sources11
Beta strandi215 – 218Combined sources4
Helixi219 – 234Combined sources16
Beta strandi240 – 243Combined sources4
Beta strandi246 – 248Combined sources3
Helixi256 – 264Combined sources9
Turni265 – 267Combined sources3
Beta strandi269 – 282Combined sources14
Helixi285 – 303Combined sources19
Beta strandi308 – 314Combined sources7
Turni318 – 320Combined sources3
Helixi323 – 326Combined sources4
Beta strandi334 – 336Combined sources3
Helixi344 – 353Combined sources10
Beta strandi382 – 385Combined sources4
Beta strandi388 – 403Combined sources16
Beta strandi405 – 407Combined sources3
Beta strandi409 – 417Combined sources9
Beta strandi419 – 421Combined sources3
Beta strandi423 – 435Combined sources13
Beta strandi438 – 443Combined sources6
Helixi446 – 448Combined sources3
Beta strandi452 – 463Combined sources12
Beta strandi465 – 467Combined sources3
Beta strandi474 – 476Combined sources3
Beta strandi479 – 483Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07986.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 352GH10PROSITE-ProRule annotationAdd BLAST311
Domaini375 – 484CBM2PROSITE-ProRule annotationAdd BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni357 – 376Linker ("hinge") (Pro-Thr box)Add BLAST20

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation
Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105D9F. Bacteria.
COG3693. LUCA.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001000. GH10.
IPR031158. GH10_AS.
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. GH10_1. 1 hit.
PS51760. GH10_2. 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.
PIRiA24994.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi590998.Celf_1271.

Protein family/group databases

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

Proteomic databases

PRIDEiP07986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105D9F. Bacteria.
COG3693. LUCA.

Miscellaneous databases

EvolutionaryTraceiP07986.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001000. GH10.
IPR031158. GH10_AS.
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. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.