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Reviewed, UniProtKB/Swiss-Prot P37696 (GUNA_ACEXY)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable endoglucanase
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase
    Cellulase
Gene names
Name: cmcAX
OrganismAcetobacter xylinus (Gluconacetobacter xylinus)
Taxonomic identifier28448 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter

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Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Enzyme capable of hydrolyzing carboxy-methyl-cellulose (CMC).

Catalytic activity

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

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 8 (cellulase D) family.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1
Chain21 – 342322Probable endoglucanase
PRO_0000007930

Sites

Active site571Proton donor By similarity
Active site1141Nucleophile Potential

Secondary structure

1 ......................................................... 342
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P37696-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 85FF9BDF8B979F81

FASTA34237,443
        10         20         30         40         50         60 
MSVMAAMGGA QVLSSTGAFA DPAPDAVAQQ WAIFRAKYLR PSGRVVDTGN GGESHSEGQG 

        70         80         90        100        110        120 
YGMLFAASAG DLASFQSMWM WARTNLQHTN DKLFSWRFLK GHQPPVPDKN NATDGDLLIA 

       130        140        150        160        170        180 
LALGRAGKRF QRPDYIQDAM AIYGDVLNLM TMKAGPYVVL MPGAVGFTKK DSVILNLSYY 

       190        200        210        220        230        240 
VMPSLLQAFD LTADPRWRQV MEDGIRLVSA GRFGQWRLPP DWLAVNRATG ALSIASGWPP 

       250        260        270        280        290        300 
RFSYDAIRVP LYFYWAHMLA PNVLADFTRF WNNFGANALP GWVDLTTGAR SPYNAPPGYL 

       310        320        330        340 
AVAECTGLDS AGELPTLDHA PDYYSAALTL LVYIARAEET IK

« Hide

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References

[1]"A new gene required for cellulose production and a gene encoding cellulolytic activity in Acetobacter xylinum are colocalized with the bcs operon."
Standal R., Iversen T.-G., Coucheron D.H., Fjaervik E., Blatny J.M., Valla S.
J. Bacteriol. 176:665-672(1994) [PubMed: 8300521] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-34.
Strain: ATCC 23769 / NCIB 8246.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M96060 Unassigned DNA. Translation: AAA16969.1.
PIRA36963.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WZZX-ray1.65A21-342[»]
ModBaseSearch...

Protein family/group databases

CAZyGH8. Glycoside Hydrolase Family 8.

Family and domain databases

InterProIPR012341. 6hp_glycosidase.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
PfamPF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSPR00735. GLHYDRLASE8.
PROSITEPS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGUNA_ACEXY
AccessionPrimary (citable) accession number: P37696
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents