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O74168

- MANBA_ASPAC

UniProt

O74168 - MANBA_ASPAC

Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. Releases the terminal mannose residue from mannotriose and is somewaht less active on other mannooligosaccharides.1 Publication

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.1 Publication

    pH dependencei

    Optimum pH is 2.0. Stable from pH 4 to pH 7.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei482 – 4821Proton 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.
    mycoCLAPiMND2B_ASPAC.

    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
    Synonyms:manB
    OrganismiAspergillus aculeatus
    Taxonomic identifieri5053 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    Secreted 2 Publications

    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 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 937914Beta-mannosidase APRO_0000394642Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi743 – 7431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi796 – 7961N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO74168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    2.60.40.320. 1 hit.
    3.20.20.80. 1 hit.
    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.

    O74168-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRALPTTATT LLGVLFFPSA SRSQYVRDLG TEQWTLSSAT LNRTVPAQFP    50
    SQVHMDLLRE GIIDEPYNDL NDFNLRWIAD ANWTYTSGKI EGLGEDYEST 100
    WLVFDGLDTF ASISFCGQFV GATDNQFRQY MFDVSSILKA CPEEPTLGIQ 150
    FGSAPNIVDA IAQDPSSPTW PEGVQITYEY PNRWFMRKEQ SDFGWDWGPA 200
    FAPAGPWKPG YVVQLKQAAP VYVRNTDLDI YRLGQINYLP PDQTQPWVVN 250
    ASLDYLGSLP ENPSMAIEVK DLQSGEILAS RPLTNITVTE GSVTGVTVLE 300
    GVDPKLWWPQ GLGDQNLYNV TISVTDGGNQ SVAEVTKRTG FRTIFLNQRN 350
    ITDAQLAQGI APGANWHFEV NGHEFYAKGS NLIPPDCFWT RVTEDTMTRL 400
    FDAVVAGNQN MLRVWSSGAY LHDYIYDLAD EKGILLCSEF QFSDALYPTD 450
    DAFLENVAAE VVYNVRRVNH HPSLALWAGG NEIESLMLLL VEAADPESYP 500
    FYVGEYEKMY ISLFLPLVYE NTRSISYSPS STTEGYLDID LSAPVPMAER 550
    YSNTTEGEYY GDTDHYNYDA SIAFDYGTYP VGRFANEFGF HSMPSLQTWQ 600
    QALTDPADLT FNSSVVMLRN HHYPAGGLMT DNYHNTVARH GRNDPGRAGL 650
    LPDAQHSVRP RGQLQRLVPR DPALPGGPLQ VTNPVLPAGQ RAARTPARVP 700
    VLAARGHLAG ALVGGDRVRR PLEGPHYVAR DIYKPVIVSP FWNYTTGALD 750
    IYVTSDLWTA AAGSVTLTWR DLSGKPIASN GGLPTKPLPF HVGALNSTRL 800
    YRMNMKQQPL PRHEDAILAL ELTATGSLPN TDEEVTFTHE QWFTPAFPKD 850
    LDLVNLRVRV EYDAPLGKFA VEATAGVALY TWLEHPEGVV GYFEENSFVV 900
    VPGQKKVVGF VVQADETDGE WVHDVTVRSL WDLNEGE 937
    Length:937
    Mass (Da):104,216
    Last modified:November 1, 1998 - v1
    Checksum:i0F6200BEB03D704B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015509 Genomic DNA. Translation: BAA29029.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015509 Genomic DNA. Translation: BAA29029.1 .

    3D structure databases

    ProteinModelPortali O74168.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.
    mycoCLAPi MND2B_ASPAC.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. 1 hit.
    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. "Cloning and sequencing of beta-mannosidase gene from Aspergillus aculeatus no. F-50."
      Takada G., Kawaguchi T., Kaga T., Sumitani J., Arai M.
      Biosci. Biotechnol. Biochem. 63:206-209(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 55-71; 186-189; 265-274; 411-424 AND 805-819, GLYCOSYLATION, SUBCELLULAR LOCATION.
      Strain: F-50.
    2. "Purification and properties of a beta-mannosidase from Aspergillus aculeatus."
      Arai M., Fujimoto H., Ooi T., Ogura S., Murao S.
      J. Appl. Glycosci. 42:49-51(1995)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
      Strain: F-50.

    Entry informationi

    Entry nameiMANBA_ASPAC
    AccessioniPrimary (citable) accession number: O74168
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 71 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

    Direct protein sequencing

    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