Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26221 (GUN4_THEFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 E-4

EC=3.2.1.4
Alternative name(s):
Cellulase E-4
Cellulase E4
Endo-1,4-beta-glucanase E-4
Gene names
Name:celD
OrganismThermobifida fusca (Thermomonospora fusca)
Taxonomic identifier2021 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length880 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

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

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

Contains 1 fibronectin type-III domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 4646 Ref.4
Chain47 – 880834Endoglucanase E-4
PRO_0000007959

Regions

Domain504 – 652149CBM3
Domain678 – 77093Fibronectin type-III
Domain771 – 880110CBM2

Sites

Active site4271 By similarity
Active site4611 By similarity
Active site4701 By similarity

Secondary structure

........................................................................................... 880
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26221 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 5EA9A6ABF45A4D9A

FASTA88095,203
        10         20         30         40         50         60 
MSVTEPPPRR RGRHSRARRF LTSLGATAAL TAGMLGVPLA TGTAHAEPAF NYAEALQKSM 

        70         80         90        100        110        120 
FFYEAQRSGK LPENNRVSWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFGF PMAFTATMLA 

       130        140        150        160        170        180 
WGAIESPEGY IRSGQMPYLK DNLRWVNDYF IKAHPSPNVL YVQVGDGDAD HKWWGPAEVM 

       190        200        210        220        230        240 
PMERPSFKVD PSCPGSDVAA ETAAAMAASS IVFADDDPAY AATLVQHAKQ LYTFADTYRG 

       250        260        270        280        290        300 
VYSDCVPAGA FYNSWSGYQD ELVWGAYWLY KATGDDSYLA KAEYEYDFLS TEQQTDLRSY 

       310        320        330        340        350        360 
RWTIAWDDKS YGTYVLLAKE TGKQKYIDDA NRWLDYWTVG VNGQRVPYSP GGMAVLDTWG 

       370        380        390        400        410        420 
ALRYAANTAF VALVYAKVID DPVRKQRYHD FAVRQINYAL GDNPRNSSYV VGFGNNPPRN 

       430        440        450        460        470        480 
PHHRTAHGSW TDSIASPAEN RHVLYGALVG GPGSPNDAYT DDRQDYVANE VATDYNAGFS 

       490        500        510        520        530        540 
SALAMLVEEY GGTPLADFPP TEEPDGPEIF VEAQINTPGT TFTEIKAMIR NQSGWPARML 

       550        560        570        580        590        600 
DKGTFRYWFT LDEGVDPADI TVSSAYNQCA TPEDVHHVSG DLYYVEIDCT GEKIFPGGQS 

       610        620        630        640        650        660 
EHRREVQFRI AGGPGWDPSN DWSFQGIGNE LAPAPYIVLY DDGVPVWGTA PEEGEEPGGG 

       670        680        690        700        710        720 
EGPGGGEEPG EDVTPPSAPG SPAVRDVTST SAVLTWSASS DTGGSGVAGY DVFLRAGTGQ 

       730        740        750        760        770        780 
EQKVGSTTRT SFTLTGLEPD TTYIAAVVAR DNAGNVSQRS TVSFTTLAEN GGGPDASCTV 

       790        800        810        820        830        840 
GYSTNDWDSG FTASIRITYH GTAPLSSWEL SFTFPAGQQV THGWNATWRQ DGAAVTATPM 

       850        860        870        880 
SWNSSLAPGA TVEVGFNGSW SGSNTPPTDF TLNGEPCALA 

« Hide

References

[1]"DNA sequences and expression in Streptomyces lividans of an exoglucanase gene and an endoglucanase gene from Thermomonospora fusca."
Jung E.D., Lao G., Irwin D., Barr B.K., Benjamin A., Wilson D.B.
Appl. Environ. Microbiol. 59:3032-3043(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YX.
[2]Wilson D.B.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora fusca."
Lao G., Ghangas G.S., Jung E.D., Wilson D.B.
J. Bacteriol. 173:3397-3407(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YX.
[4]"Cellulases of Thermomonospora fusca."
Wilson D.B.
Methods Enzymol. 160:314-323(1988)
Cited for: PROTEIN SEQUENCE OF 47-67.
[5]"Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca."
Sakon J., Irwin D., Wilson D.B., Karplus P.A.
Nat. Struct. Biol. 4:810-818(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20093 Genomic DNA. Translation: AAB42155.1.
PIRB42360.
RefSeqYP_290232.1. NC_007333.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JS4X-ray2.00A/B47-651[»]
1TF4X-ray1.90A/B47-651[»]
3TF4X-ray2.20A/B47-651[»]
4TF4X-ray2.00A/B47-651[»]
ProteinModelPortalP26221.
SMRP26221. Positions 47-651.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3580397.
KEGGtfu:Tfu_2176.

Phylogenomic databases

KOK01179.
OrthoDBEOG6KQ6BP.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
2.60.40.290. 1 hit.
2.60.40.710. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR003961. Fibronectin_type3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF00942. CBM_3. 1 hit.
PF00041. fn3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
SM01067. CBM_3. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49384. SSF49384. 2 hits.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51172. CBM3. 1 hit.
PS50853. FN3. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26221.

Entry information

Entry nameGUN4_THEFU
AccessionPrimary (citable) accession number: P26221
Secondary accession number(s): Q08167
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: December 11, 2013
This is version 104 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries