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A3DH67 (GUNS_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 44. 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:
Cellulose 1,4-beta-cellobiosidase (reducing end) CelS

EC=3.2.1.176
Alternative name(s):
Cellobiohydrolase CelS
Cellulase SS
Endo-1,4-beta-glucanase
Endoglucanase SS
Short name=EGSS
Exocellulase
Gene names
Name:celS
Ordered Locus Names:Cthe_2089
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose. Ref.3

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains. Ref.3

Enzyme regulation

Inhibited by cellobiose and lactose, but not by glucose. Ref.2

Subcellular location

Secreted.

Domain

The dockerin 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 48 (cellulase L) family.

Contains 2 dockerin domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 5-6. Ref.3

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 741714Cellulose 1,4-beta-cellobiosidase (reducing end) CelS
PRO_0000284723

Regions

Domain679 – 69921Dockerin 1
Domain711 – 73121Dockerin 2
Region251 – 2522Substrate binding By similarity
Region301 – 3022Substrate binding By similarity
Region326 – 3272Substrate binding By similarity
Region645 – 6462Substrate binding By similarity

Sites

Active site871Proton donor By similarity
Active site2551Nucleophile By similarity
Metal binding6791Calcium 1 By similarity
Metal binding6811Calcium 1 By similarity
Metal binding6831Calcium 1 By similarity
Metal binding6841Calcium 1; via amide nitrogen By similarity
Metal binding6851Calcium 1; via carbonyl oxygen By similarity
Metal binding6901Calcium 1 By similarity
Metal binding7111Calcium 2 By similarity
Metal binding7111Calcium 3 By similarity
Metal binding7121Calcium 2; via amide nitrogen By similarity
Metal binding7131Calcium 3 By similarity
Metal binding7151Calcium 3 By similarity
Metal binding7171Calcium 2; via carbonyl oxygen By similarity
Metal binding7171Calcium 3; via carbonyl oxygen By similarity
Metal binding7221Calcium 2 By similarity
Metal binding7221Calcium 3 By similarity
Binding site761Substrate By similarity
Binding site1401Substrate By similarity
Binding site2041Substrate By similarity
Binding site2411Substrate By similarity
Binding site2471Substrate By similarity
Binding site4211Substrate By similarity
Binding site5201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3DH67 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 39FDF4680BDB1144

FASTA74183,558
        10         20         30         40         50         60 
MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK IKDPKNGYFS 

        70         80         90        100        110        120 
PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG NLTGNWSGVE TAWKVMEDWI 

       130        140        150        160        170        180 
IPDSTEQPGM SSYNPNSPAT YADEYEDPSY YPSELKFDTV RVGSDPVHND LVSAYGPNMY 

       190        200        210        220        230        240 
LMHWLMDVDN WYGFGTGTRA TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK 

       250        260        270        280        290        300 
DRSYAKQWRY TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD 

       310        320        330        340        350        360 
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG YQNPFQGWVS 

       370        380        390        400        410        420 
ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG GATNSWNGRY EKYPAGTSTF 

       430        440        450        460        470        480 
YGMAYVPHPV YADPGSNQWF GFQAWSMQRV MEYYLETGDS SVKNLIKKWV DWVMSEIKLY 

       490        500        510        520        530        540 
DDGTFAIPSD LEWSGQPDTW TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER 

       550        560        570        580        590        600 
WEGKLDTKAR DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP 

       610        620        630        640        650        660 
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL AVAMGVLATY 

       670        680        690        700        710        720 
FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR SGISINTDNA DLNEDGRVNS 

       730        740 
TDLGILKRYI LKEIDTLPYK N 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and DNA sequence of the gene coding for Clostridium thermocellum cellulase Ss (CelS), a major cellulosome component."
Wang W.K., Kruus K., Wu J.H.D.
J. Bacteriol. 175:1293-1302(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37; 412-431 AND 589-605.
[2]"Product inhibition of the recombinant CelS, an exoglucanase component of the Clostridium thermocellum cellulosome."
Kruus K., Andreacchi A., Wang W.K., Wu J.H.D.
Appl. Microbiol. Biotechnol. 44:399-404(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME REGULATION.
[3]"Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component."
Kruus K., Wang W.K., Ching J., Wu J.H.
J. Bacteriol. 177:1641-1644(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06942 Genomic DNA. Translation: AAA23226.1.
CP000568 Genomic DNA. Translation: ABN53296.1.
PIRA47063.
RefSeqYP_001038489.1. NC_009012.1.

3D structure databases

ProteinModelPortalA3DH67.
SMRA3DH67. Positions 28-669, 673-741.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_2089.

Protein family/group databases

CAZyGH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN53296; ABN53296; Cthe_2089.
GeneID4810949.
KEGGcth:Cthe_2089.
PATRIC19518092. VBICloThe47081_2217.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG10655.
HOGENOMHOG000020369.
OMAGMHWLLD.
OrthoDBEOG64V28H.
ProtClustDBCLSK801496.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-2150-MONOMER.
MetaCyc:MONOMER-16423.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view]
PfamPF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSPR00844. GLHYDRLASE48.
SUPFAMSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNS_CLOTH
AccessionPrimary (citable) accession number: A3DH67
Secondary accession number(s): P38686
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: December 11, 2013
This is version 44 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