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Q4WAH4

- MANBB_ASPFU

UniProt

Q4WAH4 - MANBB_ASPFU

Protein

Beta-mannosidase B

Gene

mndB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      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.

    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:AFUA_7G01320
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 7

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 845845Beta-mannosidase BPRO_0000394654Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi723 – 7231N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00001205.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WAH4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000186861.
    KOiK01192.
    OMAiSWGLGYY.
    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.

    Q4WAH4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKLQQFPLS KGWSFRDNEA TSEDAWMPVP VVPSVVHQDL QANNKLKDPY    50
    IGFNELEARW VNEKSWTYKT VFQKPAAPAG SCIVLAFDGL DTFAKVKLDG 100
    NVILENDNMF LARRVDVTKA LEAEGDHVLE IDFDCAFLRA KELRKQDPRH 150
    NWASFNGDPS RLSVRKAQYH WGWDWGPVLM TAGIWREVRL EVYSARVADL 200
    WTEVQLASDH QSAQVTAFVE VESVHSGSHR ACFTLSLHGQ EITREEIGVT 250
    ENGTAKATFD VKEPSLWWPH GYGDATLYEV SVSLVKEQEE LHRVSKKFGI 300
    RTAEVIQRPD KHGKSFFFRV NGVDIFCGGS CWIPADNLLP SITAERYRKW 350
    IELMVHGRQV MIRVWGGGIY EDNSFYDACD ELGVLVWQDF MFGCGNYPTW 400
    PNLLESIRKE SVYNVRRLRH HPSIVIWVGN NEDYQVQEQA GLTYNYEDKD 450
    PENWLKTDFP ARYIYEKLLP EVVQEYSPGT FYHPGSPWGD GKTTSDPTVG 500
    DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI DYFVENEADK 550
    YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHIYL TQVVQAETMM 600
    FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA 650
    RVLNPIAVGV RREHHDWSVT HAQPPKTSKF ELWVASSRQQ EIQGTVELRF 700
    LSVNTGLEVR ERIVHENVSI VPNGTTNLIV DGLIDHTVHS EPHVLAARIW 750
    VDGQLVARDV DWPQPFKYLD LSDRGLEVKK ISESEDEQTL LISTKKPVKC 800
    LVFEEREGVR ISDSAMDIVP GDDQRVTIKG LKPGDAPLKY KFLGQ 845
    Length:845
    Mass (Da):96,998
    Last modified:July 5, 2005 - v1
    Checksum:iB6EA86796A8C33DE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000015 Genomic DNA. Translation: EAL84762.1.
    RefSeqiXP_746800.1. XM_741707.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00001205; CADAFUAP00001205; CADAFUAG00001205.
    GeneIDi3504183.
    KEGGiafm:AFUA_7G01320.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000015 Genomic DNA. Translation: EAL84762.1 .
    RefSeqi XP_746800.1. XM_741707.1.

    3D structure databases

    ProteinModelPortali Q4WAH4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00001205.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00001205 ; CADAFUAP00001205 ; CADAFUAG00001205 .
    GeneIDi 3504183.
    KEGGi afm:AFUA_7G01320.

    Phylogenomic databases

    eggNOGi COG3250.
    HOGENOMi HOG000186861.
    KOi K01192.
    OMAi SWGLGYY.
    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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiMANBB_ASPFU
    AccessioniPrimary (citable) accession number: Q4WAH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 64 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