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Q9UUZ3 (MANBA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length931 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 mannobiose and mannotriose, as well as from galactosyl-mannobiose (GM2), galactosyl-mannotriose (GM3) and di-galactosyl-mannopentaose (G2M5). Ref.1 Ref.2 Ref.3 UniProtKB O00462

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. Ref.1 Ref.2

Pathway

Glycan metabolism; N-glycan degradation. UniProtKB O00462

Subunit structure

Homodimer. Ref.2

Subcellular location

Secreted Ref.2.

Post-translational modification

N-glycosylated. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase A subfamily. UniProtKB O00462

Biophysicochemical properties

Kinetic parameters:

kcat is 4048 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.

KM=0.3 mM for p-nitrophenyl-beta-mannopyranoside Ref.2

pH dependence:

Optimum pH is 2.5-5.

Temperature dependence:

Optimum temperature is 70 degrees Celsius. Ref.2

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate catabolic process

Inferred from direct assay Ref.2Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Non-traceable author statement Ref.2. Source: UniProtKB

   Molecular_functionbeta-mannosidase activity

Inferred from direct assay Ref.2Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 931910Beta-mannosidase A
PRO_0000012168

Sites

Active site4791Proton donor By similarity UniProtKB P08236

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation6081N-linked (GlcNAc...) Potential
Glycosylation6581N-linked (GlcNAc...) Potential
Glycosylation7381N-linked (GlcNAc...) Potential
Glycosylation7901N-linked (GlcNAc...) Potential
Glycosylation7981N-linked (GlcNAc...) Potential
Glycosylation8301N-linked (GlcNAc...) Potential
Glycosylation9181N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9UUZ3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D296E185EA3BF430

FASTA931104,390
        10         20         30         40         50         60 
MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ VHLDLLRAGV 

        70         80         90        100        110        120 
IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV FDGLDTFATI SILWTANRIH 

       130        140        150        160        170        180 
GQSVSPVSGS MYLPALEACQ RRILIRKVSF RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR 

       190        200        210        220        230        240 
WFMRKEQSDF GWDWGPAFAP AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ 

       250        260        270        280        290        300 
SQPWVVNASI DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN 

       310        320        330        340        350        360 
PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE VQRAQGIAPG 

       370        380        390        400        410        420 
ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA VVVGNQNMLR VWSSGAYLHD 

       430        440        450        460        470        480 
YIYDLADEKG ILLWSEFEFS DALYPSDDAF LENVAAEIVY NVRRVNHHPS LALWAGGNEI 

       490        500        510        520        530        540 
ESLMLPRVKD AAPSSYSYYV GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA 

       550        560        570        580        590        600 
PVPMAERYDN TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV 

       610        620        630        640        650        660 
DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP SKSDHISNFS 

       670        680        690        700        710        720 
AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE DIWQAPSWAG IEYGGRWKVL 

       730        740        750        760        770        780 
HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK 

       790        800        810        820        830        840 
SVPFTVGGLN STRIYGTNVS SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS 

       850        860        870        880        890        900 
WPKDLKIVDP GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK 

       910        920        930 
EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G 

« Hide

References

[1]"Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation."
Ademark P., de Vries R.P., Haegglund P., Staalbrand H., Visser J.
Eur. J. Biochem. 268:2982-2990(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger."
Ademark P., Lundqvist J., Haegglund P., Tenkanen M., Torto N., Tjerneld F., Staalbrand H.
J. Biotechnol. 75:281-289(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 490-504, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION.
Strain: ATCC 46890.
[3]"Phylogenetic analysis and substrate specificity of GH2 beta-mannosidases from Aspergillus species."
Reddy S.K., Rosengren A., Klaubauf S., Kulkarni T., Karlsson E.N., de Vries R.P., Stalbrand H.
FEBS Lett. 587:3444-3449(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ251874 Genomic DNA. Translation: CAB63902.1.

3D structure databases

ProteinModelPortalQ9UUZ3.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL5417.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.
mycoCLAPMND2A_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17577.
UniPathwayUPA00280.

Family and domain databases

Gene3D3.20.20.80. 2 hits.
InterProIPR008979. Galactose-bd-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBA_ASPNG
AccessionPrimary (citable) accession number: Q9UUZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 66 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