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P29719 (GUNA_PAELA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 75. 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
EG-A
Endo-1,4-beta-glucanase
Gene names
Name:celA
OrganismPaenibacillus lautus (Bacillus lautus)
Taxonomic identifier1401 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Post-translational modification

A short form (EG-A-S) arises from post-translational proteolysis of approximately 150 AA at the C-terminus of EG-A-L.

Sequence similarities

Belongs to the glycosyl hydrolase 44 (cellulase J) family.

Contains 1 CBM3 (carbohydrate binding type-3) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
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 – 3333 Potential
Chain34 – 700667Endoglucanase A
PRO_0000008021

Regions

Domain550 – 700151CBM3

Sites

Active site2131 By similarity

Sequences

Sequence LengthMass (Da)Tools
P29719 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 3D5C8CADA53EEE0F

FASTA70076,910
        10         20         30         40         50         60 
MKTRQRKRLF VSAALAVSLT MTVPMPASVN AAASDVTFTI NTQSERAAIS PNIYGTNQDL 

        70         80         90        100        110        120 
SGTENWSSRR LGGNRLTGYN WENNASSAGR DWLHYSDDFL CGNGGVPDTD CDKPGAVVTA 

       130        140        150        160        170        180 
FHDKSLENGA YSIVTLQMAG YVSRDKNGPV DESETAPSPR WDKVEFAKNA PFSLQPHLND 

       190        200        210        220        230        240 
GQVYMDEEVN FLVNRYGNAS TSTGIKAYSL DNEPALWSET HPRIHPEQLQ AAELVAKSID 

       250        260        270        280        290        300 
LSKAVKNVDP HAEIFGPALY GFGAYLSLQD APGWPSLQGN YSWFIDYYLD QMKNAHTQNG 

       310        320        330        340        350        360 
KRLLDVLDVH WYPEAQGGGQ RIVFGGAGNI DTQKARVQAP RSLWDPAYQE DSWIGTWFSS 

       370        380        390        400        410        420 
YLPLIPKLQS SIQTYYPGTK LAITESSYGG DNHISGGIAT ADALGIFGKY GVYAANYWQT 

       430        440        450        460        470        480 
EDNTDYTSAA YKLYRNYDGN KSGFGSIKVD AATSDTENSS VYASVTDEEN SELHLIVLNK 

       490        500        510        520        530        540 
NFDDPINATF QLSGDKTYTS GRVWGFDQTG SDITEQAAIT NINNNQFTYT LPPLSAYHIV 

       550        560        570        580        590        600 
LKADSTEPVN SDLVVQYKDG DRNNATDNQI KPHFNIQNKG TSPVDLSSLT LRYYFTKDSS 

       610        620        630        640        650        660 
AAMNGWIDWA KLGGSNIQIS FGNHNGADSD TYAELGFSSG AGSIAEGGQS GEIQLRMSKA 

       670        680        690        700 
DWSNFNEAND YSFDGAKTAY IDWDRVTLYQ DGQLVWGIEP 

« Hide

References

[1]"celA from Bacillus lautus PL236 encodes a novel cellulose-binding endo-beta-1,4-glucanase."
Hansen C.K., Diderichsen B., Joergensen P.L.
J. Bacteriol. 174:3522-3531(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PL236.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76588 Genomic DNA. Translation: AAA22303.1.
PIRB41897.

3D structure databases

ProteinModelPortalP29719.
SMRP29719. Positions 33-543.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH44. Glycoside Hydrolase Family 44.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.710. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR024745. Glyco_hydro_44.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00942. CBM_3. 1 hit.
PF12891. Glyco_hydro_44. 1 hit.
[Graphical view]
SMARTSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51172. CBM3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_PAELA
AccessionPrimary (citable) accession number: P29719
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 16, 2013
This is version 75 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