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Q8WPJ2 (MANA_MYTED) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. 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:
Mannan endo-1,4-beta-mannosidase

EC=3.2.1.78
Alternative name(s):
Beta-mannanase
Endo-beta-1,4-mannanase
Short name=Man5A
Short name=ManA
OrganismMytilus edulis (Blue mussel)
Taxonomic identifier6550 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5), and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and less preferentially to mannotetraose M4; hydrolyzes M4 preferentially to M3, and less preferentially to mannose (M1), plus very little M2. Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan, starch, cellulose or galactose. Ref.1 Ref.2 Ref.4

Catalytic activity

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

Subunit structure

Monomer. Ref.2

Post-translational modification

The disulfide bond between Cys-192 and Cys-259 has not been observed in x-ray crystallograghy (Ref.4). This may be a consequence of the X-ray radiation.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=2.49 mM for mannotetraose Ref.2 Ref.4

KM=1.61 mM for mannopentaose

KM=0.5 mM for mannohexaose

pH dependence:

Optimum pH is 5.2.

Temperature dependence:

Optimum temperature is about 50 degrees Celsius.

Mass spectrometry

Molecular mass is 39702 Da from positions 18 - 367. Determined by MALDI. Ref.2

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmannan catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionmannan endo-1,4-beta-mannosidase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.2
Chain18 – 367350Mannan endo-1,4-beta-mannosidase Ref.2
PRO_0000007901

Sites

Active site1771Proton donor By similarity UniProtKB P07985
Active site3081Nucleophile By similarity UniProtKB P07985

Amino acid modifications

Disulfide bond192 ↔ 259 Probable

Experimental info

Sequence conflict681I → M no nucleotide entry Ref.4
Sequence conflict3511I → M no nucleotide entry Ref.4

Secondary structure

.................................................................. 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WPJ2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B364E03418D2EA86

FASTA36740,957
        10         20         30         40         50         60 
MLLTALAVLF ASTGCQARLS VSGTNLNYNG HHIFLSGANQ AWVNYARDFG HNQYSKGKST 

        70         80         90        100        110        120 
FESTLSDIQS HGGNSVRVWL HIEGESTPEF DNNGYVTGID NTLISDMRAY LHAAQRHNIL 

       130        140        150        160        170        180 
IFFTLWNGAV KQSTHYRLNG LMVDTRKLQS YIDHALKPMA NALKNEKALG GWDIMNEPEG 

       190        200        210        220        230        240 
EIKPGESSSE PCFDTRHLSG SGAGWAGHLY SAQEIGRFVN WQAAAIKEVD PGAMVTVGSW 

       250        260        270        280        290        300 
NMKADTDAMG FHNLYSDHCL VKAGGKQSGT LSFYQVHTYD WQNHFGNESP FKHSFSNFRL 

       310        320        330        340        350        360 
KKPMVIGEFN QEHGAGMSSE SMFEWAYTKG YSGAWTWSRT DVSWNNQLRG IQHLKSRTDH 


GQVQFGL 

« Hide

References

[1]"Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) beta-mannanase gene."
Xu B., Sellos D., Janson J.-C.
Eur. J. Biochem. 269:1753-1760(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Tissue: Digestive gland and Gill.
[2]"endo-beta-1,4-mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action."
Xu B., Hagglund P., Stalbrand H., Janson J.-C.
J. Biotechnol. 92:267-277(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-53, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
Tissue: Digestive gland.
[3]"Crystallization and X-ray analysis of native and selenomethionyl beta-mannanase Man5A from blue mussel, Mytilus edulis, expressed in Pichia pastoris."
Xu B., Munoz I.G., Janson J.-C., Stahlberg J.
Acta Crystallogr. D 58:542-545(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[4]"Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis."
Larsson A.M., Anderson L., Xu B., Munoz I.G., Uson I., Janson J.-C., Stalbrand H., Stahlberg J.
J. Mol. Biol. 357:1500-1510(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-367, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271365 Genomic DNA. Translation: CAC81056.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C0HX-ray1.60A15-367[»]
ProteinModelPortalQ8WPJ2.
SMRQ8WPJ2. Positions 18-367.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8WPJ2.

Entry information

Entry nameMANA_MYTED
AccessionPrimary (citable) accession number: Q8WPJ2
Secondary accession number(s): P82544, P82801
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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