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P54583 (GUN1_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 E1

EC=3.2.1.4
Alternative name(s):
Cellulase E1
Endo-1,4-beta-glucanase E1
Endocellulase E1
Gene names
Ordered Locus Names:Acel_0614
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a very high specific activity on carboxymethylcellulose.

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.

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

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 81 degrees Celsius. Thermostable.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 562521Endoglucanase E1
PRO_0000007834

Regions

Domain458 – 562105CBM2
Region42 – 400359Catalytic
Compositional bias401 – 46161Pro/Ser/Thr-rich (linker)

Sites

Active site2031Proton donor
Active site3231Nucleophile

Amino acid modifications

Disulfide bond75 ↔ 161
Disulfide bond209 ↔ 212

Secondary structure

......................................................................... 562
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54583 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 84E6256406A35041

FASTA56260,748
        10         20         30         40         50         60 
MPRALRRVPG SRVMLRVGVV VAVLALVAAL ANLAVPRPAR AAGGGYWHTS GREILDANNV 

        70         80         90        100        110        120 
PVRIAGINWF GFETCNYVVH GLWSRDYRSM LDQIKSLGYN TIRLPYSDDI LKPGTMPNSI 

       130        140        150        160        170        180 
NFYQMNQDLQ GLTSLQVMDK IVAYAGQIGL RIILDRHRPD CSGQSALWYT SSVSEATWIS 

       190        200        210        220        230        240 
DLQALAQRYK GNPTVVGFDL HNEPHDPACW GCGDPSIDWR LAAERAGNAV LSVNPNLLIF 

       250        260        270        280        290        300 
VEGVQSYNGD SYWWGGNLQG AGQYPVVLNV PNRLVYSAHD YATSVYPQTW FSDPTFPNNM 

       310        320        330        340        350        360 
PGIWNKNWGY LFNQNIAPVW LGEFGTTLQS TTDQTWLKTL VQYLRPTAQY GADSFQWTFW 

       370        380        390        400        410        420 
SWNPDSGDTG GILKDDWQTV DTVKDGYLAP IKSSIFDPVG ASASPSSQPS PSVSPSPSPS 

       430        440        450        460        470        480 
PSASRTPTPT PTPTASPTPT LTPTATPTPT ASPTPSPTAA SGARCTASYQ VNSDWGNGFT 

       490        500        510        520        530        540 
VTVAVTNSGS VATKTWTVSW TFGGNQTITN SWNAAVTQNG QSVTARNMSY NNVIQPGQNT 

       550        560 
TFGFQASYTG SNAAPTVACA AS 

« Hide

References

« Hide 'large scale' references
[1]Laymon R.A., Himmel M.E., Thomas S.R.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.
[3]"Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose."
Sakon J., Adney W.S., Himmel M.E., Thomas S.R., Kaplus P.A.
Biochemistry 35:10648-10660(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-398.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33212 Genomic DNA. Translation: AAA75477.1.
CP000481 Genomic DNA. Translation: ABK52387.1.
RefSeqYP_872373.1. NC_008578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECEX-ray2.40A/B42-399[»]
1VRXX-ray2.40A/B42-399[»]
ProteinModelPortalP54583.
SMRP54583. Positions 42-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351607.Acel_0614.

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK52387; ABK52387; Acel_0614.
GeneID4486396.
KEGGace:Acel_0614.
PATRIC20671622. VBIAciCel132453_0657.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000225207.
KOK01179.
OMATHGRATH.
OrthoDBEOG6FRCSN.
ProtClustDBCLSK2532842.

Enzyme and pathway databases

BioCycACEL351607:GIXW-627-MONOMER.

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54583.

Entry information

Entry nameGUN1_ACIC1
AccessionPrimary (citable) accession number: P54583
Secondary accession number(s): A0LSH7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 13, 2013
This is version 95 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries