Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P37700 (GUNG_CLOCE)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Endoglucanase G
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase G
    Cellulase G
    EGCCG
Gene names
Name: celCCG
Ordered Locus Names: Ccel_0731
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Hide | Top

Protein attributes

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

Hide | Top

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 residues 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.

Hide | Top

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

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

1 ............................................................................................... 725
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P37700-1 [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

Hide | Top

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: 1398087] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium cellulolyticum H10."
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].
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

M87018 Genomic DNA. Translation: AAA73868.1.
CP001348 Genomic DNA. Translation: ACL75110.1.
PIRJC1300.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1G87X-ray1.60A/B36-649[»]
1GA2X-ray1.70A/B36-649[»]
1K72X-ray1.80A/B36-649[»]
1KFGX-ray1.90A/B36-649[»]
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.4. 97402.

Family and domain databases

ProDomPD001947. CBD_3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit. Uncertain.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents