Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 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. Involved in the degradation of polymeric mannan and galactomannan. Releases the terminal mannose residue from mannobiose and mannotriose, as well as from galactosyl-mannobiose (GM2), galactosyl-mannotriose (GM3) and di-galactosyl-mannopentaose (G2M5).2 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.2 Publications

Kineticsi

kcat is 4048 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.

  1. KM=0.3 mM for p-nitrophenyl-beta-mannopyranoside1 Publication

    pH dependencei

    Optimum pH is 2.5-5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei479 – 4791Proton donorBy similarity

    GO - Molecular functioni

    • beta-mannosidase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17577.
    UniPathwayiUPA00280.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.
    mycoCLAPiMND2A_ASPNG.

    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
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 931910Beta-mannosidase APRO_0000012168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi738 – 7381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi798 – 7981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi830 – 8301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi918 – 9181N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UUZ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 2 hits.
    InterProiIPR008979. Galactose-bd-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UUZ3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ
    60 70 80 90 100
    VHLDLLRAGV IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV
    110 120 130 140 150
    FDGLDTFATI SILWTANRIH GQSVSPVSGS MYLPALEACQ RRILIRKVSF
    160 170 180 190 200
    RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR WFMRKEQSDF GWDWGPAFAP
    210 220 230 240 250
    AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ SQPWVVNASI
    260 270 280 290 300
    DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN
    310 320 330 340 350
    PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE
    360 370 380 390 400
    VQRAQGIAPG ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA
    410 420 430 440 450
    VVVGNQNMLR VWSSGAYLHD YIYDLADEKG ILLWSEFEFS DALYPSDDAF
    460 470 480 490 500
    LENVAAEIVY NVRRVNHHPS LALWAGGNEI ESLMLPRVKD AAPSSYSYYV
    510 520 530 540 550
    GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA PVPMAERYDN
    560 570 580 590 600
    TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV
    610 620 630 640 650
    DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP
    660 670 680 690 700
    SKSDHISNFS AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE
    710 720 730 740 750
    DIWQAPSWAG IEYGGRWKVL HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS
    760 770 780 790 800
    DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK SVPFTVGGLN STRIYGTNVS
    810 820 830 840 850
    SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS WPKDLKIVDP
    860 870 880 890 900
    GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK
    910 920 930
    EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G
    Length:931
    Mass (Da):104,390
    Last modified:May 1, 2000 - v1
    Checksum:iD296E185EA3BF430
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ251874 Genomic DNA. Translation: CAB63902.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ251874 Genomic DNA. Translation: CAB63902.1.

    3D structure databases

    ProteinModelPortaliQ9UUZ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    ChEMBLiCHEMBL5417.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.
    mycoCLAPiMND2A_ASPNG.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00280.
    BioCyciMetaCyc:MONOMER-17577.

    Family and domain databases

    Gene3Di3.20.20.80. 2 hits.
    InterProiIPR008979. Galactose-bd-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation."
      Ademark P., de Vries R.P., Haegglund P., Staalbrand H., Visser J.
      Eur. J. Biochem. 268:2982-2990(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
    2. "Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger."
      Ademark P., Lundqvist J., Haegglund P., Tenkanen M., Torto N., Tjerneld F., Staalbrand H.
      J. Biotechnol. 75:281-289(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 490-504, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION.
      Strain: ATCC 46890.
    3. "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, SUBSTRATE SPECIFICITY.
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

    Entry informationi

    Entry nameiMANBA_ASPNG
    AccessioniPrimary (citable) accession number: Q9UUZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 67 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

    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.