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Protein

Beta-mannosidase B

Gene

mndB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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. Releases the terminal mannose residue from mannobiose, mannotriose and galactosyl-mannotriose (GM3), but not from galactosyl-mannobiose (GM2) or di-galactosyl-mannopentaose (G2M5).2 Publications

Catalytic activityi

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

Kineticsi

kcat is 79.2 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.

  1. KM=0.22 mM for p-nitrophenyl-beta-mannopyranoside1 Publication

    pH dependencei

    Optimum pH is 6. Active from pH 5 to 8.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius (at pH 6).1 Publication

    Pathway: N-glycan degradation

    This protein is involved in the pathway N-glycan degradation, which is part of Glycan metabolism.
    View all proteins of this organism that are known to be involved in the pathway N-glycan degradation and in Glycan metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei432 – 4321Proton donorBy similarity

    GO - Molecular functioni

    • beta-mannosidase activity Source: UniProtKB

    GO - Biological processi

    • mannan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00280.

    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:AN3368
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560 Componenti: Chromosome VI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 843843Beta-mannosidase BPRO_0000394658Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00009674.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B7W2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000186861.
    InParanoidiQ5B7W2.
    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.
    IPR006103. Glyco_hydro_2_TIM.
    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.
    PF02836. Glyco_hydro_2_C. 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.

    Q5B7W2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF
    60 70 80 90 100
    IGLNELSARW VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG
    110 120 130 140 150
    QVILESDNMF LAHRVDITKA LDVEGEHTLE IDFDCALLRA RELRKQHPDH
    160 170 180 190 200
    KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM TAGIWKEVRL EVYSAKISDL
    210 220 230 240 250
    WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG QQIGKEVATL
    260 270 280 290 300
    DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI
    310 320 330 340 350
    RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW
    360 370 380 390 400
    IELMAVGHQV MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW
    410 420 430 440 450
    PEILESIEKE AEYNLRRLRH HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD
    460 470 480 490 500
    PESWLKTDFP ARYIYEHLLP KAVQKIIPSA YYHPGSPWGD GKITSDPTVG
    510 520 530 540 550
    DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI DHFVTNEADK
    560 570 580 590 600
    YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM
    610 620 630 640 650
    FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS
    660 670 680 690 700
    RVLKPLAIGV RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF
    710 720 730 740 750
    ISIKTGLAIH ESIVRENVTI VPNGTTNILD GVIDHAVDEP HVLAARLWVD
    760 770 780 790 800
    GELVARDVDW PQPFKYLDLS DRGLEITRIS KTESEQVLEL SARKPVKCLV
    810 820 830 840
    FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF LGQ
    Length:843
    Mass (Da):96,367
    Last modified:June 15, 2010 - v2
    Checksum:i53B99E1C93DB4055
    GO

    Sequence cautioni

    The sequence CBF82847.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence EAA63336.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ490488 mRNA. Translation: ABF50864.1.
    AACD01000055 Genomic DNA. Translation: EAA63336.1. Sequence problems.
    BN001306 Genomic DNA. Translation: CBF82847.1. Sequence problems.
    RefSeqiXP_660972.1. XM_655880.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00009674; CADANIAP00009674; CADANIAG00009674.
    GeneIDi2874350.
    KEGGiani:AN3368.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ490488 mRNA. Translation: ABF50864.1.
    AACD01000055 Genomic DNA. Translation: EAA63336.1. Sequence problems.
    BN001306 Genomic DNA. Translation: CBF82847.1. Sequence problems.
    RefSeqiXP_660972.1. XM_655880.1.

    3D structure databases

    ProteinModelPortaliQ5B7W2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00009674.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiCADANIAT00009674; CADANIAP00009674; CADANIAG00009674.
    GeneIDi2874350.
    KEGGiani:AN3368.2.

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000186861.
    InParanoidiQ5B7W2.
    KOiK01192.
    OrthoDBiEOG7NSB9Q.

    Enzyme and pathway databases

    UniPathwayiUPA00280.

    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.
    IPR006103. Glyco_hydro_2_TIM.
    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.
    PF02836. Glyco_hydro_2_C. 1 hit.
    PF02837. Glyco_hydro_2_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49303. SSF49303. 2 hits.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "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, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.

    Entry informationi

    Entry nameiMANBB_EMENI
    AccessioniPrimary (citable) accession number: Q5B7W2
    Secondary accession number(s): C8VHQ6, Q1HFT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: June 24, 2015
    This is version 69 of the entry and version 2 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.1 Publication

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.