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P37700 (GUNG_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase G

EC=3.2.1.4
Alternative name(s):
Cellulase G
EGCCG
Endo-1,4-beta-glucanase G
Gene names
Name:celCCG
Ordered Locus Names:Ccel_0731
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Pathway

Glycan metabolism; cellulose degradation.

Domain

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Contains 1 CBM3 (carbohydrate binding type-3) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 725690Endoglucanase G
PRO_0000007947

Regions

Domain489 – 650162CBM3
Repeat664 – 687241
Repeat696 – 719242
Region664 – 719562 X 24 AA approximate repeats

Sites

Active site4081 By similarity
Active site4461 By similarity
Active site4551 By similarity

Experimental info

Sequence conflict609 – 6102TT → RR in AAA73868. Ref.1

Secondary structure

............................................................................................... 725
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37700 [UniParc].

Last modified May 26, 2009. Version 2.
Checksum: 1C87FE4D03797C41

FASTA72579,776
        10         20         30         40         50         60 
MLKTKRKLTK AIGVALSISI LSSLVSFIPQ TNTYAAGTYN YGEALQKSIM FYEFQRSGDL 

        70         80         90        100        110        120 
PADKRDNWRD DSGMKDGSDV GVDLTGGWYD AGDHVKFNLP MSYTSAMLAW SLYEDKDAYD 

       130        140        150        160        170        180 
KSGQTKYIMD GIKWANDYFI KCNPTPGVYY YQVGDGGKDH SWWGPAEVMQ MERPSFKVDA 

       190        200        210        220        230        240 
SKPGSAVCAS TAASLASAAV VFKSSDPTYA EKCISHAKNL FDMADKAKSD AGYTAASGYY 

       250        260        270        280        290        300 
SSSSFYDDLS WAAVWLYLAT NDSTYLDKAE SYVPNWGKEQ QTDIIAYKWG QCWDDVHYGA 

       310        320        330        340        350        360 
ELLLAKLTNK QLYKDSIEMN LDFWTTGVNG TRVSYTPKGL AWLFQWGSLR HATTQAFLAG 

       370        380        390        400        410        420 
VYAEWEGCTP SKVSVYKDFL KSQIDYALGS TGRSFVVGYG VNPPQHPHHR TAHGSWTDQM 

       430        440        450        460        470        480 
TSPTYHRHTI YGALVGGPDN ADGYTDEINN YVNNEIACDY NAGFTGALAK MYKHSGGDPI 

       490        500        510        520        530        540 
PNFKAIEKIT NDEVIIKAGL NSTGPNYTEI KAVVYNQTGW PARVTDKISF KYFMDLSEIV 

       550        560        570        580        590        600 
AAGIDPLSLV TSSNYSEGKN TKVSGVLPWD VSNNVYYVNV DLTGENIYPG GQSACRREVQ 

       610        620        630        640        650        660 
FRIAAPQGTT YWNPKNDFSY DGLPTTSTVN TVTNIPVYDN GVKVFGNEPA GGSENPDPEI 

       670        680        690        700        710        720 
LYGDVNSDKN VDALDFAALK KYLLGGTSSI DVKAADTYKD GNIDAIDMAT LKKYLLGTIT 


QLPQG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum."
Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P.
Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium cellulolyticum H10."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Zhou J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87018 Genomic DNA. Translation: AAA73868.1.
CP001348 Genomic DNA. Translation: ACL75110.1.
PIRJC1300.
RefSeqYP_002505090.1. NC_011898.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G87X-ray1.60A/B36-649[»]
1GA2X-ray1.70A/B36-649[»]
1K72X-ray1.80A/B36-649[»]
1KFGX-ray1.90A/B36-649[»]
ProteinModelPortalP37700.
SMRP37700. Positions 37-649.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394503.Ccel_0731.

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL75110; ACL75110; Ccel_0731.
GeneID7309585.
KEGGcce:Ccel_0731.
PATRIC19432259. VBICloCel57783_0756.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG05134.
HOGENOMHOG000021032.
OMATAASGYY.
OrthoDBEOG6KQ6BP.
ProtClustDBCLSK702792.

Enzyme and pathway databases

BioCycCCEL394503:GJET-752-MONOMER.
UniPathwayUPA00696.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR016134. Cellulos_enz_dockerin_1.
IPR018242. Dockerin_1.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamPF00942. CBM_3. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37700.

Entry information

Entry nameGUNG_CLOCE
AccessionPrimary (citable) accession number: P37700
Secondary accession number(s): B8I7V3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries