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O74168 (MANBA_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:
Beta-mannosidase A

EC=3.2.1.25
Alternative name(s):
Mannanase A
Short name=Mannase A
Gene names
Name:mndA
Synonyms:manB
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan. Releases the terminal mannose residue from mannotriose and is somewaht less active on other mannooligosaccharides. Ref.2

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. Ref.2

Pathway

Glycan metabolism; N-glycan degradation.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted Ref.1 Ref.2.

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase A subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 2.0. Stable from pH 4 to pH 7. Ref.2

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-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 – 2323 Potential
Chain24 – 937914Beta-mannosidase A
PRO_0000394642

Sites

Active site4821Proton donor By similarity

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3191N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Glycosylation7431N-linked (GlcNAc...) Potential
Glycosylation7961N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O74168 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 0F6200BEB03D704B

FASTA937104,216
        10         20         30         40         50         60 
MRALPTTATT LLGVLFFPSA SRSQYVRDLG TEQWTLSSAT LNRTVPAQFP SQVHMDLLRE 

        70         80         90        100        110        120 
GIIDEPYNDL NDFNLRWIAD ANWTYTSGKI EGLGEDYEST WLVFDGLDTF ASISFCGQFV 

       130        140        150        160        170        180 
GATDNQFRQY MFDVSSILKA CPEEPTLGIQ FGSAPNIVDA IAQDPSSPTW PEGVQITYEY 

       190        200        210        220        230        240 
PNRWFMRKEQ SDFGWDWGPA FAPAGPWKPG YVVQLKQAAP VYVRNTDLDI YRLGQINYLP 

       250        260        270        280        290        300 
PDQTQPWVVN ASLDYLGSLP ENPSMAIEVK DLQSGEILAS RPLTNITVTE GSVTGVTVLE 

       310        320        330        340        350        360 
GVDPKLWWPQ GLGDQNLYNV TISVTDGGNQ SVAEVTKRTG FRTIFLNQRN ITDAQLAQGI 

       370        380        390        400        410        420 
APGANWHFEV NGHEFYAKGS NLIPPDCFWT RVTEDTMTRL FDAVVAGNQN MLRVWSSGAY 

       430        440        450        460        470        480 
LHDYIYDLAD EKGILLCSEF QFSDALYPTD DAFLENVAAE VVYNVRRVNH HPSLALWAGG 

       490        500        510        520        530        540 
NEIESLMLLL VEAADPESYP FYVGEYEKMY ISLFLPLVYE NTRSISYSPS STTEGYLDID 

       550        560        570        580        590        600 
LSAPVPMAER YSNTTEGEYY GDTDHYNYDA SIAFDYGTYP VGRFANEFGF HSMPSLQTWQ 

       610        620        630        640        650        660 
QALTDPADLT FNSSVVMLRN HHYPAGGLMT DNYHNTVARH GRNDPGRAGL LPDAQHSVRP 

       670        680        690        700        710        720 
RGQLQRLVPR DPALPGGPLQ VTNPVLPAGQ RAARTPARVP VLAARGHLAG ALVGGDRVRR 

       730        740        750        760        770        780 
PLEGPHYVAR DIYKPVIVSP FWNYTTGALD IYVTSDLWTA AAGSVTLTWR DLSGKPIASN 

       790        800        810        820        830        840 
GGLPTKPLPF HVGALNSTRL YRMNMKQQPL PRHEDAILAL ELTATGSLPN TDEEVTFTHE 

       850        860        870        880        890        900 
QWFTPAFPKD LDLVNLRVRV EYDAPLGKFA VEATAGVALY TWLEHPEGVV GYFEENSFVV 

       910        920        930 
VPGQKKVVGF VVQADETDGE WVHDVTVRSL WDLNEGE 

« Hide

References

[1]"Cloning and sequencing of beta-mannosidase gene from Aspergillus aculeatus no. F-50."
Takada G., Kawaguchi T., Kaga T., Sumitani J., Arai M.
Biosci. Biotechnol. Biochem. 63:206-209(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 55-71; 186-189; 265-274; 411-424 AND 805-819, GLYCOSYLATION, SUBCELLULAR LOCATION.
Strain: F-50.
[2]"Purification and properties of a beta-mannosidase from Aspergillus aculeatus."
Arai M., Fujimoto H., Ooi T., Ogura S., Murao S.
J. Appl. Glycosci. 42:49-51(1995)
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Strain: F-50.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015509 Genomic DNA. Translation: BAA29029.1.

3D structure databases

ProteinModelPortalO74168.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.
mycoCLAPMND2B_ASPAC.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBA_ASPAC
AccessionPrimary (citable) accession number: O74168
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 70 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries