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P25472 (GUND_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 D

EC=3.2.1.4
Alternative name(s):
Cellulase D
EGCCD
Endo-1,4-beta-glucanase D
Gene names
Name:celCCD
Ordered Locus Names:Ccel_0840
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 5 (cellulase A) family.

Contains 1 CBM11 (carbohydrate binding type-11) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 584560Endoglucanase D
PRO_0000007846

Regions

Domain354 – 584231CBM11
Repeat530 – 552231
Repeat562 – 584232
Region25 – 328304Catalytic By similarity
Region530 – 584552 X 24 AA approximate repeats
Compositional bias329 – 35325Pro/Thr-rich (linker)

Sites

Active site1591Proton donor By similarity
Active site2641Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P25472 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 0FC41257E81322C3

FASTA58466,062
        10         20         30         40         50         60 
MKKILALIIS CSIIMSFLPM SVYGAINSQD MVKKMGIGMN LGNTFDAPTE GSWSKAAQEY 

        70         80         90        100        110        120 
YFDDFKQAGF KHVRIPIRWD QHTLANSPYT VDSNFLNRIE TVIDWSLSRG FVTVINSHHD 

       130        140        150        160        170        180 
TWLMDNYSQN IGRFEKIWEQ IAQRFKGKSE NLVFEILNEP HGNITDSQIN DMNKRILNII 

       190        200        210        220        230        240 
RKTNPTRNVI IGAGYWNSYN SLSQLEIPND PNLIATFHYY DPYSFTHQWQ GTWGTKNDMD 

       250        260        270        280        290        300 
AIAMVFNHVK KWSDKNNIPV YLGEYGVMGH SDRTSAVKWF DFVSDQAISH GFSCGAWDNG 

       310        320        330        340        350        360 
VFGSVDNDMA FYNRDTRQFD KEILNAILTT GTTYDWTPPT ETNPDPPRTP ATPAYGEQLI 

       370        380        390        400        410        420 
EDFEGAMQWA AYSGVDATAS CKISSGKSNN GLEITYAGSS NGYWGVVDNE HRNQDWEKWQ 

       430        440        450        460        470        480 
KISFDIKSSN TNEVRLLIAE QSKIEGEDGE HWTYVIKPST SWTTIEIPFS SFTKRMDYQP 

       490        500        510        520        530        540 
PAQDGSETFD LYKVGSLHFM YSNSNSGTLN IDNIKLIGLP EEQIGGKIGD VNEDGNIDAI 

       550        560        570        580 
DFALLKKYLL DSSISINKVN ADINLDGDIN AIDFAKLKMM LLGD 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence analysis of the endoglucanase-encoding gene, celCCD, of Clostridium cellulolyticum."
Shima S., Igarashi Y., Kodama T.
Gene 104:33-38(1991) [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90341 Genomic DNA. Translation: BAA14354.1.
CP001348 Genomic DNA. Translation: ACL75216.1.
RefSeqYP_002505196.1. NC_011898.1.

3D structure databases

ProteinModelPortalP25472.
SMRP25472. Positions 354-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394503.Ccel_0840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL75216; ACL75216; Ccel_0840.
GeneID7309687.
KEGGcce:Ccel_0840.
PATRIC19432493. VBICloCel57783_0870.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2730.
KOK01179.
OMADATASCK.
OrthoDBEOG66F040.
ProtClustDBCLSK625314.

Enzyme and pathway databases

BioCycCCEL394503:GJET-865-MONOMER.
UniPathwayUPA00696.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProIPR005087. CBM_fam11.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUND_CLOCE
AccessionPrimary (citable) accession number: P25472
Secondary accession number(s): B8I8I3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 19, 2014
This is version 101 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries