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Protein

Endoglucanase B

Gene

celB

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei276 – 2761NucleophilePROSITE-ProRule annotation
Active sitei393 – 3931Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-374-MONOMER.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH45. Glycoside Hydrolase Family 45.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase B (EC:3.2.1.4)
Short name:
EGB
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:celB
Synonyms:cel45A
Ordered Locus Names:CJA_0374
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 511482Endoglucanase BPRO_0000008023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 127By similarity
Disulfide bondi181 ↔ 212By similarity
Disulfide bondi191 ↔ 206By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_0374.

Structurei

3D structure databases

ProteinModelPortaliP18126.
SMRiP18126. Positions 177-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 130101CBM2Add
BLAST
Domaini180 – 20728CBM10Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi132 – 17342Ser-rich (linker)Add
BLAST
Compositional biasi223 – 25937Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000066289.
OMAiFANEMEN.
OrthoDBiEOG6QCDJD.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.40.40.10. 1 hit.
2.60.40.290. 1 hit.
InterProiIPR014733. 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]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF02015. Glyco_hydro_45. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF50685. SSF50685. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLLSGWVRP LMLGCGLLGA ALSAGSIQAA VCEYRVTNEW GSGFTASIRI
60 70 80 90 100
TNNGSSTING WSVSWNYTDG SRVTSSWNAG LSGANPYSAT PVGWNTSIPI
110 120 130 140 150
GSSVEFGVQG NNGSSRAQVP AVTGAICGGQ GSSAPSSVAS SSSSSSVVSS
160 170 180 190 200
TPRSSSSSVS SSVPGTSSSS SSSVLTGAQA CNWYGTLTPL CNNTSNGWGY
210 220 230 240 250
EDGRSCVART TCSAQPAPYG IVSTSSSTPL SSSSSSRSSV ASSSSLSSAT
260 270 280 290 300
SSSASSVSSV PPIDGGCNGY ATRYWDCCKP HCGWSANVPS LVSPLQSCSA
310 320 330 340 350
NNTRLSDVSV GSSCDGGGGY MCWDKIPFAV SPTLAYGYAA TSSGDVCGRC
360 370 380 390 400
YQLQFTGSSY NAPGDPGSAA LAGKTMIVQA TNIGYDVSGG QFDILVPGGG
410 420 430 440 450
VGAFNACSAQ WGVSNAELGA QYGGFLAACK QQLGYNASLS QYKSCVLNRC
460 470 480 490 500
DSVFGSRGLT QLQQGCTWFA EWFEAADNPS LKYKEVPCPA ELTTRSGMNR
510
SILNDIRNTC P
Length:511
Mass (Da):52,078
Last modified:November 1, 1990 - v1
Checksum:i3C3119D998291D8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52615 Genomic DNA. Translation: CAA36844.1.
CP000934 Genomic DNA. Translation: ACE82688.1.
PIRiS10527.

Genome annotation databases

EnsemblBacteriaiACE82688; ACE82688; CJA_0374.
KEGGicja:CJA_0374.
PATRICi21324125. VBICelJap122165_0383.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52615 Genomic DNA. Translation: CAA36844.1.
CP000934 Genomic DNA. Translation: ACE82688.1.
PIRiS10527.

3D structure databases

ProteinModelPortaliP18126.
SMRiP18126. Positions 177-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_0374.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH45. Glycoside Hydrolase Family 45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACE82688; ACE82688; CJA_0374.
KEGGicja:CJA_0374.
PATRICi21324125. VBICelJap122165_0383.

Phylogenomic databases

HOGENOMiHOG000066289.
OMAiFANEMEN.
OrthoDBiEOG6QCDJD.

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-374-MONOMER.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.40.40.10. 1 hit.
2.60.40.290. 1 hit.
InterProiIPR014733. 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]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF02015. Glyco_hydro_45. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF50685. SSF50685. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGUNB_CELJU
AccessioniPrimary (citable) accession number: P18126
Secondary accession number(s): B3PI35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 22, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.