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P23550 (GUNB_PAELA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. 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 B

EC=3.2.1.4
Alternative name(s):
Cellulase B
Endo-1,4-beta-glucanase B
Short name=EG-B
Gene names
Name:celB
OrganismPaenibacillus lautus (Bacillus lautus)
Taxonomic identifier1401 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length566 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.

Sequence similarities

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

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030
Chain31 – 566536Endoglucanase B
PRO_0000007835

Sites

Active site1771Proton donor By similarity
Active site2991Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P23550 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 6426C8D8E29022C9

FASTA56662,622
        10         20         30         40         50         60 
MKKRRSSKVI LSLAIVVALL AAVEPNAALA AAPPSAMQSY VEAMQPGWNL GNSLDAVGAD 

        70         80         90        100        110        120 
ETLARGNPRI TKELIQNIAA QGYKSIRIPV TWDSHIGAAP NYQIEAAYLN RVQEVVQWAL 

       130        140        150        160        170        180 
DANLYVMINV HHDSWLWISK MESQHDQVLA RYNAIWTQIA NKFKNSPSKL MFESVNEPRF 

       190        200        210        220        230        240 
TDGGTTDEAK QQKMLDELNV SFFNIVRNSG GQNATRPLVL STLEASPTQE RMTALYNTMT 

       250        260        270        280        290        300 
KLNDKNLIAT VHFYGFWPFS VNIAGYTKFD AETQNDIITT FDNVYNTFVA KGIPVVVGEY 

       310        320        330        340        350        360 
GLLGFDKNTG VIEQGEKLKF FEFFAQYVKQ KSISTMLWDN GQHFNRTSFK WSDPDLFNMI 

       370        380        390        400        410        420 
KASWTGRSST ASSDLIHVKQ GTAVKDTSVQ LNLNGNTLTS LSVNGTTLKS GTDYTLNSSR 

       430        440        450        460        470        480 
LTFKASQLTK LTSLGKLGVN ATIVTKFNRG ADWKFNVVLY NTPKLSSTTG TTSSFAIPTA 

       490        500        510        520        530        540 
FNGDQLATME AVYVNGGNAG PHNWTSFKEF ETTFSPAYSE GKIKLQQAFF NEVNDTTVTL 

       550        560 
KFQFWSGEIV NYTIKKSGST VTGTAS 

« Hide

References

[1]"Multiple endo-beta-1,4-glucanase-encoding genes from Bacillus lautus PL236 and characterization of the celB gene."
Joergensen P.L., Hansen C.K.
Gene 93:55-60(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PL236.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33762 Genomic DNA. Translation: AAA22408.1.
PIRJH0218.

3D structure databases

ProteinModelPortalP23550.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM46. Carbohydrate-Binding Module Family 46.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProIPR005102. Carbo-bd_X2.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR016282. Glyco_hydro_5_endoGlcnase_B.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF03442. CBM_X2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
PIRSFPIRSF001043. Endoglucanase_B. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNB_PAELA
AccessionPrimary (citable) accession number: P23550
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 16, 2013
This is version 72 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