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P18126 (GUNB_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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

Short name=EGB
EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:celB
Synonyms:cel45A
Ordered Locus Names:CJA_0374
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. EGB is most active against barley beta-glucan, but showed significant activity against amorphous and crystalline cellulose.

Catalytic activity

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

Subcellular location

Periplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 45 (cellulase K) family.

Contains 1 CBM10 (carbohydrate binding type-10) domain.

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 2929 Ref.1
Chain30 – 511482Endoglucanase B
PRO_0000008023

Regions

Domain30 – 130101CBM2
Domain180 – 20728CBM10
Compositional bias132 – 17342Ser-rich (linker)
Compositional bias223 – 25937Ser-rich

Sites

Active site2761Nucleophile By similarity
Active site3931Proton donor By similarity

Amino acid modifications

Disulfide bond32 ↔ 127 By similarity
Disulfide bond181 ↔ 212 By similarity
Disulfide bond191 ↔ 206 By similarity

Sequences

Sequence LengthMass (Da)Tools
P18126 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 3C3119D998291D8E

FASTA51152,078
        10         20         30         40         50         60 
MNLLSGWVRP LMLGCGLLGA ALSAGSIQAA VCEYRVTNEW GSGFTASIRI TNNGSSTING 

        70         80         90        100        110        120 
WSVSWNYTDG SRVTSSWNAG LSGANPYSAT PVGWNTSIPI GSSVEFGVQG NNGSSRAQVP 

       130        140        150        160        170        180 
AVTGAICGGQ GSSAPSSVAS SSSSSSVVSS TPRSSSSSVS SSVPGTSSSS SSSVLTGAQA 

       190        200        210        220        230        240 
CNWYGTLTPL CNNTSNGWGY EDGRSCVART TCSAQPAPYG IVSTSSSTPL SSSSSSRSSV 

       250        260        270        280        290        300 
ASSSSLSSAT SSSASSVSSV PPIDGGCNGY ATRYWDCCKP HCGWSANVPS LVSPLQSCSA 

       310        320        330        340        350        360 
NNTRLSDVSV GSSCDGGGGY MCWDKIPFAV SPTLAYGYAA TSSGDVCGRC YQLQFTGSSY 

       370        380        390        400        410        420 
NAPGDPGSAA LAGKTMIVQA TNIGYDVSGG QFDILVPGGG VGAFNACSAQ WGVSNAELGA 

       430        440        450        460        470        480 
QYGGFLAACK QQLGYNASLS QYKSCVLNRC DSVFGSRGLT QLQQGCTWFA EWFEAADNPS 

       490        500        510 
LKYKEVPCPA ELTTRSGMNR SILNDIRNTC P 

« Hide

References

« Hide 'large scale' references
[1]"The N-terminal region of an endoglucanase from Pseudomonas fluorescens subspecies cellulosa constitutes a cellulose-binding domain that is distinct from the catalytic centre."
Gilbert H.J., Hall J., Hazlewood G.P., Ferreira L.M.A.
Mol. Microbiol. 4:759-767(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-48.
[2]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52615 Genomic DNA. Translation: CAA36844.1.
CP000934 Genomic DNA. Translation: ACE82688.1.
PIRS10527.
RefSeqYP_001980898.1. NC_010995.1.

3D structure databases

ProteinModelPortalP18126.
SMRP18126. Positions 177-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498211.CJA_0374.

Protein family/group databases

CAZyCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH45. Glycoside Hydrolase Family 45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE82688; ACE82688; CJA_0374.
GeneID6416065.
KEGGcja:CJA_0374.
PATRIC21324125. VBICelJap122165_0383.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000066289.
OMAFANEMEN.
OrthoDBEOG6QCDJD.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-374-MONOMER.

Family and domain databases

Gene3D2.30.32.30. 1 hit.
2.40.40.10. 1 hit.
2.60.40.290. 1 hit.
InterProIPR014733. Barwin-like_endoglucanase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR000334. Glyco_hydro_45.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF02015. Glyco_hydro_45. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF50685. SSF50685. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNB_CELJU
AccessionPrimary (citable) accession number: P18126
Secondary accession number(s): B3PI35
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 14, 2014
This is version 98 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