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P26414 (GUNA_THEBI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 75. 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 A

EC=3.2.1.4
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene names
Name:celA
OrganismThermobispora bispora (Microbispora bispora)
Taxonomic identifier2006 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeThermobispora

Protein attributes

Sequence length456 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 6 (cellulase B) family.

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
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 – 3030 Potential
Chain31 – 456426Endoglucanase A
PRO_0000007905

Regions

Domain353 – 456104CBM2
Region31 – 322292Catalytic
Region323 – 35533Linker ("hinge") (Pro-Ser box)

Sites

Active site1131 By similarity
Active site1511Proton donor By similarity
Active site3001Nucleophile By similarity

Amino acid modifications

Disulfide bond114 ↔ 159 By similarity
Disulfide bond267 ↔ 302 By similarity
Disulfide bond360 ↔ 453 By similarity

Sequences

Sequence LengthMass (Da)Tools
P26414 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B06D8595E322848F

FASTA45647,011
        10         20         30         40         50         60 
MSRIRRFLAT ALAAATAGVG AIVTAIASAG PAHAYDSPFY VDPQSNAAKW VAANPNDPRT 

        70         80         90        100        110        120 
PVIRDRIAAV PTGRWFANYN PSTVRAEVDA YVGAAAAAGK IPIMVVYAMP NRDCGGPSAG 

       130        140        150        160        170        180 
GAPNHTAYRA WIDEIAAGLR NRPAVIILEP DALPIMTNCM SPSEQAEVQA SAVGAGKKFK 

       190        200        210        220        230        240 
AASSQAKVYF DAGHDAWVPA DEMASRLRGA DIANSADGIA LNVSNYRYTS GLISYAKSVL 

       250        260        270        280        290        300 
SAIGASHLRA VIDTSRNGNG PLGSEWCDPP GRATGTWSTT DTGDPAIDAF LWIKPPGEAD 

       310        320        330        340        350        360 
GCIATPGVFV PDRAYELAMN AAPPTYSPSP TPSTPSPSPS QSDPGSPSPS PSQPPAGRAC 

       370        380        390        400        410        420 
EATYALVNQW PGGFQAEVTV KNTGSSPING WTVQWTLPSG QSITQLWNGD LSTSGSNVTV 

       430        440        450 
RNVSWNGNVP AGGSTSFGFL GSGTGQLSSS ITCSAS 

« Hide

References

[1]Yablonsky M.D., Elliston K.O., Eveleigh D.E.
(In) Coughlan M.P. (eds.); Production, characterization and application of cellulose, hemicellulose and lignin enzyme degrading systems, pp.77-83, Elsevier, London (1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

3D structure databases

ProteinModelPortalP26414.
SMRP26414. Positions 36-321, 356-449.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSPR00733. GLHYDRLASE6.
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_THEBI
AccessionPrimary (citable) accession number: P26414
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 16, 2013
This is version 75 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