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A2QYN2

- MANBB_ASPNC

UniProt

A2QYN2 - MANBB_ASPNC

Protein

Beta-mannosidase B

Gene

mndB

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 2 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. Prefers manobiose over mannotriose and has no activity against polymeric mannan. Is also severly restricetd by galactosyl substitutions at the +1 subsite 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 sitei432 – 4321Proton donorBy similarity

    GO - Molecular functioni

    1. beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. mannan catabolic process Source: InterPro

    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 B (EC:3.2.1.25)
    Alternative name(s):
    Mannanase B
    Short name:
    Mannase B
    Gene namesi
    Name:mndB
    ORF Names:An12g01850
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 3L

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 844844Beta-mannosidase BPRO_0000394655Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi723 – 7231N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00009453.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QYN2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000186861.
    KOiK01192.
    OrthoDBiEOG7NSB9Q.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    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.
    IPR006104. Glyco_hydro_2_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR028369. Mannanase.
    [Graphical view]
    PANTHERiPTHR10066:SF12. PTHR10066:SF12. 1 hit.
    PfamiPF00703. Glyco_hydro_2. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49303. SSF49303. 2 hits.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2QYN2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAFAQYTLS TGWYFKDRDE LASEAWMPVP VVPSVVHQDL QANGKLKNPY    50
    VGFNELDARW VNEKSWTYRK ILQKPTVLAG SRIVLAFDGL DTFAKVKLDN 100
    NIILESSNMF QAYRVDVTKA LDCGDEHVLE IEFDCAMLRA QELRKQDPNH 150
    NWASFNGDPA RMSVRKAQYH WGWDWGPVLM TAGIWRAVRL EVYSTRLADL 200
    WTEINLDPTH KTASISAFTE LESVDLDPSY KVKFTITLHG KQIAQAEATP 250
    QEGRAKVEFN IDQPCLWWPH GYGDSTLYEV SASLNADQLE LHRVTKKIGI 300
    RTAEVVQRPD KHGKSFFFRI NGVDIFCGGS CWIPADNLLP NISPQRYRKW 350
    IQLMVAGRQA MIRVWGGGCY EDDSFYEACD ELGVLVWQDF MFGCGNYPTW 400
    PELLKSIEQE AIYNVRRLRH HPSIVVYVGN NEDYQVQEQA GLEYNYEDKN 450
    PENWLKTNFP ARYIYEELLP SVVERCSPKT FYHPGSPWGD GKITSDPTVG 500
    DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHLSTI EYFVENEKDK 550
    YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYIYL TQVVQAETMM 600
    FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAYYAVA 650
    RVLNPVAVGV RREHHDWSIT HAQPPKTSKY ELWVVSSLQK PASGKVELRF 700
    LSVDTGREIR ERIVRENVDI VPNGTTNLIT DGLIDHTVDA EPHVLAARLW 750
    VDGEIVARDV DWPQPFKYLD FADRGLEVKR VSEASDQQVF QISTEKPVKC 800
    LVFEERDGVK FSDSAMDIVP GDVQTVKVTG LRADEKLKYK FLGQ 844
    Length:844
    Mass (Da):97,117
    Last modified:March 6, 2007 - v1
    Checksum:iD24AE1CB82B9CEA0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270263 Genomic DNA. Translation: CAK48467.1.
    RefSeqiXP_001395271.1. XM_001395234.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00009634; CADANGAP00009453; CADANGAG00009634.
    GeneIDi4985535.
    KEGGiang:ANI_1_250104.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270263 Genomic DNA. Translation: CAK48467.1 .
    RefSeqi XP_001395271.1. XM_001395234.2.

    3D structure databases

    ProteinModelPortali A2QYN2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00009453.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00009634 ; CADANGAP00009453 ; CADANGAG00009634 .
    GeneIDi 4985535.
    KEGGi ang:ANI_1_250104.

    Phylogenomic databases

    eggNOGi COG3250.
    HOGENOMi HOG000186861.
    KOi K01192.
    OrthoDBi EOG7NSB9Q.

    Enzyme and pathway databases

    UniPathwayi UPA00280 .

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    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.
    IPR006104. Glyco_hydro_2_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR028369. Mannanase.
    [Graphical view ]
    PANTHERi PTHR10066:SF12. PTHR10066:SF12. 1 hit.
    Pfami PF00703. Glyco_hydro_2. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49303. SSF49303. 2 hits.
    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 nameiMANBB_ASPNC
    AccessioniPrimary (citable) accession number: A2QYN2
    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

    Miscellaneous

    In contrast to clade A beta-mannosidases, which are likely secreted, clade B proteins appear to be intracellular.By similarity

    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