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Q9UUZ3

- MANBA_ASPNG

UniProt

Q9UUZ3 - MANBA_ASPNG

Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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).2 Publications

    Catalytic activityi

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

    Kineticsi

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

    1. KM=0.3 mM for p-nitrophenyl-beta-mannopyranoside1 Publication

    pH dependencei

    Optimum pH is 2.5-5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei479 – 4791Proton donorBy similarity

    GO - Molecular functioni

    1. beta-mannosidase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17577.
    UniPathwayiUPA00280.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.
    mycoCLAPiMND2A_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-mannosidase A (EC:3.2.1.25)
    Alternative name(s):
    Mannanase A
    Short name:
    Mannase A
    Gene namesi
    Name:mndA
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 931910Beta-mannosidase APRO_0000012168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi738 – 7381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi798 – 7981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi830 – 8301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi918 – 9181N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UUZ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 2 hits.
    InterProiIPR008979. Galactose-bd-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UUZ3-1 [UniParc]FASTAAdd to Basket

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    MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ    50
    VHLDLLRAGV IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV 100
    FDGLDTFATI SILWTANRIH GQSVSPVSGS MYLPALEACQ RRILIRKVSF 150
    RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR WFMRKEQSDF GWDWGPAFAP 200
    AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ SQPWVVNASI 250
    DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN 300
    PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE 350
    VQRAQGIAPG ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA 400
    VVVGNQNMLR VWSSGAYLHD YIYDLADEKG ILLWSEFEFS DALYPSDDAF 450
    LENVAAEIVY NVRRVNHHPS LALWAGGNEI ESLMLPRVKD AAPSSYSYYV 500
    GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA PVPMAERYDN 550
    TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV 600
    DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP 650
    SKSDHISNFS AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE 700
    DIWQAPSWAG IEYGGRWKVL HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS 750
    DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK SVPFTVGGLN STRIYGTNVS 800
    SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS WPKDLKIVDP 850
    GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK 900
    EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G 931
    Length:931
    Mass (Da):104,390
    Last modified:May 1, 2000 - v1
    Checksum:iD296E185EA3BF430
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ251874 Genomic DNA. Translation: CAB63902.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ251874 Genomic DNA. Translation: CAB63902.1 .

    3D structure databases

    ProteinModelPortali Q9UUZ3.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL5417.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.
    mycoCLAPi MND2A_ASPNG.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00280 .
    BioCyci MetaCyc:MONOMER-17577.

    Family and domain databases

    Gene3Di 3.20.20.80. 2 hits.
    InterProi IPR008979. Galactose-bd-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiMANBA_ASPNG
    AccessioniPrimary (citable) accession number: Q9UUZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3