Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5B7W2

- MANBB_EMENI

UniProt

Q5B7W2 - MANBB_EMENI

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: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. beta-mannosidase activity Source: UniProtKB

    GO - Biological processi

    1. mannan catabolic process Source: UniProtKB

    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: 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.
    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

    MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF    50
    IGLNELSARW VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG 100
    QVILESDNMF LAHRVDITKA LDVEGEHTLE IDFDCALLRA RELRKQHPDH 150
    KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM TAGIWKEVRL EVYSAKISDL 200
    WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG QQIGKEVATL 250
    DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI 300
    RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW 350
    IELMAVGHQV MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW 400
    PEILESIEKE AEYNLRRLRH HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD 450
    PESWLKTDFP ARYIYEHLLP KAVQKIIPSA YYHPGSPWGD GKITSDPTVG 500
    DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI DHFVTNEADK 550
    YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM 600
    FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS 650
    RVLKPLAIGV RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF 700
    ISIKTGLAIH ESIVRENVTI VPNGTTNILD GVIDHAVDEP HVLAARLWVD 750
    GELVARDVDW PQPFKYLDLS DRGLEITRIS KTESEQVLEL SARKPVKCLV 800
    FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF LGQ 843
    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.
    The sequence EAA63336.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490488 mRNA. Translation: ABF50864.1 .
    AACD01000055 Genomic DNA. Translation: EAA63336.1 . Sequence problems.
    BN001306 Genomic DNA. Translation: CBF82847.1 . Sequence problems.
    RefSeqi XP_660972.1. XM_655880.1.

    3D structure databases

    ProteinModelPortali Q5B7W2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00009674.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00009674 ; CADANIAP00009674 ; CADANIAG00009674 .
    GeneIDi 2874350.
    KEGGi ani:AN3368.2.

    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.
    IPR006103. Glyco_hydro_2_TIM.
    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.
    PF02836. Glyco_hydro_2_C. 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. "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: October 1, 2014
    This is version 65 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