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P51529 (MANA_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 70. 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
Gene names
Name:manA
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Contains 1 CBM10 (carbohydrate binding type-10) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.8.

Temperature dependence:

Optimum temperature is 58 degrees Celsius.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncellulose binding

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 – 3535 Ref.1
Chain36 – 383348Mannan endo-1,4-beta-mannosidase
PRO_0000007900

Regions

Domain345 – 37531CBM10
Compositional bias336 – 3405Poly-Gly

Sequences

Sequence LengthMass (Da)Tools
P51529 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 5DB4B407C64E94C3

FASTA38339,682
        10         20         30         40         50         60 
MRNARSTLIT TAGMAFAVLG LLFALAGPSA GRAEAAAGGI HVSNGRVVEG NGSAFVMRGV 

        70         80         90        100        110        120 
NHAYTWYPDR TGSIADIAAK GANTVRVVLS SGGRWTKTSA SEVSALIGQC KANKVICVLE 

       130        140        150        160        170        180 
VHDTTGYGKD GATSLDQAGD YWVGVKSAAW RAQEDYVVVN IGNEPFGNTN YAAWTDATKS 

       190        200        210        220        230        240 
AIGKLRGAGL GHALMVDAPN WGQDWSGTMR SNAASVFASD PDRNTVFSIH MYGVYDTAAE 

       250        260        270        280        290        300 
VRDYLNAFVG NGLPIVVGEF GDQHSDGNPD EDAIMATAQS LGVGYLGWSW SGNGGGVEYL 

       310        320        330        340        350        360 
DMVNGFDPNS LTSWGNRILY GSNGIAATSR TATVYGGGGG STGGTAPNGY PYCVNGGASD 

       370        380 
PDGDGWGWEN SRSCVVRGSA ADH 

« Hide

References

[1]"Beta-mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme."
Arcand N., Kluepfel D., Paradis F.W., Morosoli R., Shareck F.
Biochem. J. 290:857-863(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-42.
Strain: 66 / 1326.
[2]Shareck F.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO C-TERMINUS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M92297 Genomic DNA. Translation: AAA26710.2.
PIRS30386.

3D structure databases

ProteinModelPortalP51529.
SMRP51529. Positions 37-336.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM10. Carbohydrate-Binding Module Family 10.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR002883. CBM10/Dockerin_dom.
IPR009031. CBM_fam10.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02013. CBM_10. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTSM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANA_STRLI
AccessionPrimary (citable) accession number: P51529
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: December 11, 2013
This is version 70 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries