Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26224 (GUNF_CLOTH) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 F

Short name=EGF
EC=3.2.1.4
Alternative name(s):
Cellulase F
Endo-1,4-beta-glucanase
Gene names
Name:celF
Ordered Locus Names:Cthe_0543
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Catalytic activity

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

Cofactor

Calcium.

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
   LigandCalcium
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 2727
Chain28 – 739712Endoglucanase F
PRO_0000007950

Regions

Domain480 – 639160CBM3
Repeat670 – 693241
Repeat709 – 732242
Region28 – 470443Catalytic
Region670 – 732632 X 24 AA approximate repeats

Sites

Active site4001 By similarity
Active site4381 By similarity
Active site4471 By similarity

Sequences

Sequence LengthMass (Da)Tools
P26224 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 0CD69EEFC6D4AEEF

FASTA73982,089
        10         20         30         40         50         60 
MKKILAFLLT VALVAVVAIP QAVVSFAADF NYGEALQKAI MFYEFQRSGK LPENKRNNWR 

        70         80         90        100        110        120 
GDSALNDGAD NGLDLTGGWY DAGDHVKFNL PMAYAVTMLA WSVYESRDAY VQSGQLPYIL 

       130        140        150        160        170        180 
DNIKWATDYF IKCHPSPNVY YYQVGDGALD HSWWGPAEVM QMPRPSFKVD LTNPGSTVVA 

       190        200        210        220        230        240 
ETAAAMAASS IVFKPTDPEY AATLLRHAKE LFTFADTTRS DAGYRAAEGY YSSHSGFYDE 

       250        260        270        280        290        300 
LTWASIWLYL ATGDQSYLDK AESYEPHWER ERGTTLISYS WAHCWDNKLY GSLLLLAKIT 

       310        320        330        340        350        360 
GKSYYKQCIE NHLDYWTVGF NGSRVQYTPK GLAYLDRWGS LRYATTQAFL ASVYADWSGC 

       370        380        390        400        410        420 
DPAKAAVYKE FAKKQVDYAL GSTGRSFVVG FGKNPPRNPH HRTAHSSWSA LMTEPAECRH 

       430        440        450        460        470        480 
ILVGALVGGP DGSDSYVDRL DDYQCNEVAN DYNAGFVGAL AKMYEKYGGE PIPNFVAFET 

       490        500        510        520        530        540 
PGEEFYVEAA VNAAGPGFVN IKASIINKSG WPARGSDKLS AKYFVDISEA VAKGITLDQI 

       550        560        570        580        590        600 
TVQSTTNGGA KVSQLLPWDP DNHIYYVNID FTGINIFPGG INEYKRDVYF TITAPYGEGN 

       610        620        630        640        650        660 
WDNTNDFSFQ GLEQGFTSKK TEYIPLYDGN VRVWGKVPDG GSEPDPTPTI TVGPTPSVTP 

       670        680        690        700        710        720 
TSVPGIMLGD VNFDGRINST DYSRLKRYVI KSLEFTDPEE HQKFIAAADV DGNGRINSTD 

       730 
LYVLNRYILK LIEKFPAEQ 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the cellulase gene celF of Clostridium thermocellum."
Navarro A., Chebrou M.-C., Beguin P., Aubert J.-P.
Res. Microbiol. 142:927-936(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.
[3]"Transcription of Clostridium thermocellum endoglucanase genes celF and celD."
Mishra S., Beguin P., Aubert J.-P.
J. Bacteriol. 173:80-85(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60545 Genomic DNA. Translation: CAA43035.1.
CP000568 Genomic DNA. Translation: ABN51779.1.
PIRI40804.
S15727.
RefSeqYP_001036972.1. NC_009012.1.

3D structure databases

ProteinModelPortalP26224.
SMRP26224. Positions 30-638.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_0543.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN51779; ABN51779; Cthe_0543.
GeneID4808292.
KEGGcth:Cthe_0543.
PATRIC19514745. VBICloThe47081_0565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG05134.
HOGENOMHOG000021032.
OMAKHNAGRT.
OrthoDBEOG6KQ6BP.
ProtClustDBCLSK702792.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-561-MONOMER.
MetaCyc:MONOMER-16419.

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.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
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. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNF_CLOTH
AccessionPrimary (citable) accession number: P26224
Secondary accession number(s): A3DCV0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries