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P07984 (GUNA_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 93. 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 A

EC=3.2.1.4
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene names
Name:cenA
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Post-translational modification

The linker region (also termed "hinge") may be a potential site for proteolysis.

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Sequence similarities

Belongs to the glycosyl hydrolase 6 (cellulase B) family.

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131Tat-type signal Potential
Chain32 – 449418Endoglucanase A
PRO_0000007903

Regions

Domain32 – 137106CBM2
Region139 – 16830Linker ("hinge") (Pro-Thr box)
Region438 – 44912Catalytic

Sites

Active site2471 By similarity
Active site2831Proton donor By similarity
Active site4231Nucleophile By similarity

Amino acid modifications

Disulfide bond35 ↔ 134 Ref.3
Disulfide bond248 ↔ 291 Ref.3
Disulfide bond390 ↔ 426 Ref.3

Sequences

Sequence LengthMass (Da)Tools
P07984 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 67FF887814B3348D

FASTA44946,731
        10         20         30         40         50         60 
MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG ANVTITNLGD 

        70         80         90        100        110        120 
PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN GSIPTGGTAS FGFNGSWAGS 

       130        140        150        160        170        180 
NPTPASFSLN GTTCTGTVPT TSPTPTPTPT TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT 

       190        200        210        220        230        240 
QGYRAWQAAS GTDKALLEKI ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV 

       250        260        270        280        290        300 
YAIPGRDCGS HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF 

       310        320        330        340        350        360 
LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS NYQTTADSKA 

       370        380        390        400        410        420 
YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER PVAVNDGSGL DALLWVKLPG 

       430        440 
ESDGACNGGP AAGQWWQEIA LEMARNARW 

« Hide

References

[1]"Characterization and structure of an endoglucanase gene cenA of Cellulomonas fimi."
Wong W.K.R., Gerhard B., Guo Z.M., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
Gene 44:315-324(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural and functional analysis of a bacterial cellulase by proteolysis."
Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
J. Biol. Chem. 264:17802-17808(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[3]"Structural and functional relationships in two families of beta-1,4-glycanases."
Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
Eur. J. Biochem. 202:367-377(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15823 Genomic DNA. Translation: AAA23084.1.
PIRA24993.

3D structure databases

ProteinModelPortalP07984.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP07984.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSPR00733. GLHYDRLASE6.
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_CELFI
AccessionPrimary (citable) accession number: P07984
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 16, 2013
This is version 93 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