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P28623 (GUND_CLOC7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 91. 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
Endo-1,4-beta-glucanase D
Gene names
Name:engD
Ordered Locus Names:Clocel_3242
OrganismClostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) [Complete proteome] [HAMAP]
Taxonomic identifier573061 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has endoglucanase activity on carboxymethyl-cellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel).

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.1
Chain32 – 515484Endoglucanase D
PRO_0000007848

Regions

Domain404 – 515112CBM2
Region32 – 376345Catalytic By similarity
Compositional bias377 – 40731Pro/Thr-rich (linker)

Sites

Active site1801Proton donor By similarity
Active site3031Nucleophile By similarity

Experimental info

Sequence conflict188 – 1892NE → LQ in AAA23233. Ref.1

Secondary structure

............................................................................. 515
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28623 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 57F15B035856008E

FASTA51555,978
        10         20         30         40         50         60 
MIKHLLSRGK LLLFVSVMAT SSIIAGGNAY GSTAFTGVRD VPAQQIVNEM KVGWNLGNTM 

        70         80         90        100        110        120 
DAIGGETNWG NPMTTHAMIN KIKEAGFNTL RLPVTWDGHM GAAPEYTIDQ TWMKRVEEIA 

       130        140        150        160        170        180 
NYAFDNDMYV IINLHHENEW LKPFYANEAQ VKAQLTKVWT QIANNFKKYG DHLIFETMNE 

       190        200        210        220        230        240 
PRPVGASNEW TGGSYENREV VNRYNLTAVN AIRATGGNNA TRYIMVPTLA ASAMSTTIND 

       250        260        270        280        290        300 
LVIPNNDSKV IVSLHMYSPY FFAMDINGTS SWGSDYDKSS LDSEFDAVYN KFVKNGRAVV 

       310        320        330        340        350        360 
IGEMGSINKN NTAARVTHAE YYAKSAKARG LTPIWWDNGY SVAGKAETFG IFNRSNLTWD 

       370        380        390        400        410        420 
APEVMKAFIK GIGGSSTTTP TTPTTPTTPT TPTTPTTPTT PTTPTTPQSA VEVTYAITNS 

       430        440        450        460        470        480 
WGSGASVNVT IKNNGTTPIN GWTLKWTMPI NQTITNMWSA SFVASGTTLS VTNAGYNGTI 

       490        500        510 
AANGGTQSFG FNINYSGVLS KPTGFTVNGT ECTVK 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction."
Hamamoto T., Foong F., Shoseyov O., Doi R.H.
Mol. Gen. Genet. 231:472-479(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-44.
[2]"Complete sequence of Clostridium cellulovorans 743B."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Hemme C.L., Woyke T.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37434 Genomic DNA. Translation: AAA23233.1.
CP002160 Genomic DNA. Translation: ADL52928.1.
PIRS20493.
RefSeqYP_003844692.1. NC_014393.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NDYX-ray2.10A/B/C/D32-376[»]
E/F/G/H409-515[»]
3NDZX-ray2.08A/B/C/D32-376[»]
E/F/G/H409-515[»]
ProteinModelPortalP28623.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL52928; ADL52928; Clocel_3242.
GeneID9610136.
KEGGccb:Clocel_3242.
PATRIC41732687. VBICloCel81632203721_0262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000027405.
OMATWGEEAT.

Enzyme and pathway databases

BioCycCCEL573061:GIXD-3329-MONOMER.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28623.

Entry information

Entry nameGUND_CLOC7
AccessionPrimary (citable) accession number: P28623
Secondary accession number(s): D9SUH3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 30, 2010
Last modified: November 13, 2013
This is version 91 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries