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A2QWU9

- MANBA_ASPNC

UniProt

A2QWU9 - MANBA_ASPNC

Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      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 By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00280.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.

    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
    ORF Names:An11g06540
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 7R

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 931910Beta-mannosidase APRO_5000220610Add
    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
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi326 – 3261N-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

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00008814.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QWU9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000216059.
    OrthoDBiEOG78D7TH.

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    2.60.40.320. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR008979. 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]
    PfamiPF00703. Glyco_hydro_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A2QWU9-1 [UniParc]FASTAAdd to Basket

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    MRHSIGLAAA LLAPTLPVAL GQYIRDLSTE KWTLSSRALN RTVPAQFPSQ    50
    VHLDLLRAGV IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYDSTWLV 100
    FDGLDTFATI SFCGQQIAST DNQFRQYAFD VSTALGSCKG DPVLSINFGS 150
    APNIVDAIAQ DSNSQKWPDD VQLTYEYPNR WFMRKEQSDF GWDWGPAFAP 200
    AGPWKPAYIV QLDKKESVYV LNTDLDIYRK GQINYLPPDQ SQPWVVNASI 250
    DILGPLPTKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLT 300
    PKLWWPQGLG DQNLYNVSIT VQSRGNQTVA SVNKRTGFRT IFLNQRNITE 350
    AQRAQGIAPG ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EEKMSRLFDA 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 MGVVSYYPIP 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
    GLKIGHSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK 900
    EISFTVLEDT TDGAWVRNIT VQSLWDQKVR G 931
    Length:931
    Mass (Da):104,026
    Last modified:March 6, 2007 - v1
    Checksum:iC3D32E4763723612
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270241 Genomic DNA. Translation: CAK96951.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00008982; CADANGAP00008814; CADANGAG00008982.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270241 Genomic DNA. Translation: CAK96951.1 .

    3D structure databases

    ProteinModelPortali A2QWU9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00008814.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00008982 ; CADANGAP00008814 ; CADANGAG00008982 .

    Phylogenomic databases

    eggNOGi COG3250.
    HOGENOMi HOG000216059.
    OrthoDBi EOG78D7TH.

    Enzyme and pathway databases

    UniPathwayi UPA00280 .

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    2.60.40.320. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR008979. 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 ]
    Pfami PF00703. Glyco_hydro_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiMANBA_ASPNC
    AccessioniPrimary (citable) accession number: A2QWU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 46 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

    Complete proteome, Reference proteome

    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