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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: N-glycan degradation

    This protein is involved in the pathway N-glycan degradation, which is part of Glycan metabolism.By similarity
    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)DescriptionActionsGraphical viewLength
    Active sitei479Proton donorBy similarity1

    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

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL5417.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 21Sequence analysisAdd BLAST21
    ChainiPRO_000001216822 – 931Beta-mannosidase AAdd BLAST910

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi40N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi79N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi247N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi282N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi347N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi550N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi608N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi658N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi738N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi790N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi798N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi830N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi918N-linked (GlcNAc...)Sequence analysis1

    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 databases

    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...

    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: January 20, 2016
    This is version 69 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

    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 one 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.