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P55278 (MANB2_BACIU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 55. 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:
Mannan endo-1,4-beta-mannosidase

EC=3.2.1.78
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase
Beta-mannanase
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processsubstituted mannan metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: InterPro

mannan endo-1,4-beta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 360336Mannan endo-1,4-beta-mannosidase
PRO_0000012171

Sequences

Sequence LengthMass (Da)Tools
P55278 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 070B0EBCC0382383

FASTA36040,295
        10         20         30         40         50         60 
MLKKLAVCLS IVLLLLGAAS PISAHTVYPV NPNAQQTTKD IMNWLAHLPN RSENRVMSGA 

        70         80         90        100        110        120 
FGGYSDVTFS MTEENRLKNA TGQSPAIYGC DYGRGWLETA DITDTIDYCC NSSLISYWKS 

       130        140        150        160        170        180 
GGLPQVSLHL ANPAFPSGNY KTAISNSQYK NILDPSTVEG KRLEALLSKI ADGLTQLKNQ 

       190        200        210        220        230        240 
GVTVLFRPLH EMNGEWFWWG LTGYNQKDNE RISLYKELYK KIYRYMTETR GLDNLLWVYS 

       250        260        270        280        290        300 
PDANRDFKTD FYPGSSYVDI TGLDAYFTDP YAISGYDEML SLKKPFAFAE TGPSGNIGSF 

       310        320        330        340        350        360 
DYAAFINAIR QKYPQTTYFL TWDEQLSPAA NQGAQSLYQN SWTLNKGEIW NGGSLTPIAE 

« Hide

References

[1]"Cloning and sequencing of beta-mannanase gene from Bacillus subtilis NM-39."
Mendoza N.S., Arai M., Sugimoto K., Ueda M., Kawaguchi T., Joson L.M.
Biochim. Biophys. Acta 1243:552-554(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NM-39.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37964 Genomic DNA. Translation: BAA07178.1.
PIRS60268.

3D structure databases

ProteinModelPortalP55278.
SMRP55278. Positions 25-360.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR016714. Mannan-1_4-b-mannosidase.
[Graphical view]
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PIRSFPIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANB2_BACIU
AccessionPrimary (citable) accession number: P55278
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 55 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