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P55296 (MANA_PIRSP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 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:
Mannan endo-1,4-beta-mannosidase A

EC=3.2.1.78
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase A
Beta-mannanase A
Gene names
Name:MANA
OrganismPiromyces sp.
Taxonomic identifier45796 [NCBI]
Taxonomic lineageEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

Protein attributes

Sequence length606 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods. Shows very high activity against mannohexaose but not against mannopentaose and smaller mannooligosaccharides. The major products released from mannooligosaccharide hydrolysis are mannose and mannobiose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.

Catalytic activity

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

Domain

Consists of a catalytic N-terminal domain linked to a reiterated non-catalytic C-terminal domain.

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Contains 3 CBM10 (carbohydrate binding type-10) domains.

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 606587Mannan endo-1,4-beta-mannosidase A
PRO_0000012174

Regions

Domain22 – 140119CBM6
Domain491 – 52636CBM10 1
Domain530 – 56536CBM10 2
Domain569 – 60436CBM10 3
Region141 – 471331Catalytic
Region472 – 48918Linker

Sequences

Sequence LengthMass (Da)Tools
P55296 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 79AAFEEFA2725D86

FASTA60668,055
        10         20         30         40         50         60 
MKSLNVILTL LSLIISVLSK KVYYEAEDGK LNGITVFKEL SGFSGKGYVG RFENPGNSVT 

        70         80         90        100        110        120 
VTVDAPATGM YDLSIIYCAN MGQKINSLTV NDQSVGDITF TENTKFETKD VGAVYLNKGK 

       130        140        150        160        170        180 
NTIGLVSSWG WMWVDAFVIN DAPNAAKDVS SKLNPTLVNP KAIPAAKKLY DFLKTNYGKR 

       190        200        210        220        230        240 
ILSGQVGAAG QAGDEGQEIQ RIQKATGKLP AVWNMDFIFE SNDCTWRPQN PDITEMAINW 

       250        260        270        280        290        300 
WKKYEGKGIM AAQWHWNIAG KTGDFAFYSK DTTFNLENAV TEGTWEYEKI IKDIDRVSGH 

       310        320        330        340        350        360 
IKKLQAVNMP LIWRPLHENN GDWFWWGNNP KACAKLWKIL YERMVNYHGL NNLIWLWNGN 

       370        380        390        400        410        420 
NDANTPVDYI DIIGVDIYAN DHGPQTTAYN THFDFYGGKK MVVLSENGRI PDIQQCVDQD 

       430        440        450        460        470        480 
VWWGYFQTWN SEFILQDSYH TDAQLKEYFN HKTVMNMDEL PSFNVDSYNG DSGSSHNGNS 

       490        500        510        520        530        540 
ESNSNTGNSD ECWSINLGYP CCIGDYVVTT DENGDWGVEN NEWCGIVHKS CWSEPLGYPC 

       550        560        570        580        590        600 
CVGNTVISAD ESGDWGVENN EWCGIVHKSC WAEFLGYPCC VGNTVISTDE FGDWGVENDD 


WCGILN 

« Hide

References

[1]"The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain."
Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.
J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91857 mRNA. Translation: CAA62968.1.

3D structure databases

ProteinModelPortalP55296.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPMAN26A_PIRSP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
3.90.1220.10. 3 hits.
InterProIPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02013. CBM_10. 3 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 3 hits.
PROSITEPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANA_PIRSP
AccessionPrimary (citable) accession number: P55296
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 11, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries