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P56526

- AGLU_ASPNG

UniProt

P56526 - AGLU_ASPNG

Protein

Alpha-glucosidase

Gene

aglA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.

    Catalytic activityi

    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei490 – 4901Nucleophile
    Active sitei493 – 4931By similarity
    Active sitei660 – 6601Proton donorBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. maltose alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.
    mycoCLAPiAGL31A_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Maltase
    Gene namesi
    Name:aglA
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 985960Alpha-glucosidasePRO_0000018576Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361O-linked (Man)1 Publication
    Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
    Glycosylationi143 – 1431N-linked (GlcNAc...)1 Publication
    Glycosylationi218 – 2181N-linked (GlcNAc...)1 Publication
    Glycosylationi347 – 3471N-linked (GlcNAc...)1 Publication
    Glycosylationi422 – 4221N-linked (GlcNAc...)1 Publication
    Glycosylationi506 – 5061N-linked (GlcNAc...)1 Publication
    Glycosylationi534 – 5341N-linked (GlcNAc...)1 Publication
    Glycosylationi537 – 5371N-linked (GlcNAc...)
    Glycosylationi545 – 5451O-linked (Man)1 Publication
    Glycosylationi550 – 5501O-linked (Man)1 Publication
    Glycosylationi559 – 5591O-linked (Man)1 Publication
    Glycosylationi560 – 5601O-linked (Man)1 Publication
    Glycosylationi561 – 5611O-linked (Man)1 Publication
    Glycosylationi562 – 5621O-linked (Man)1 Publication
    Glycosylationi571 – 5711O-linked (Man)1 Publication
    Glycosylationi601 – 6011N-linked (GlcNAc...)1 Publication
    Glycosylationi623 – 6231N-linked (GlcNAc...)1 Publication
    Glycosylationi835 – 8351N-linked (GlcNAc...)1 Publication
    Glycosylationi881 – 8811N-linked (GlcNAc...)1 Publication
    Glycosylationi895 – 8951O-linked (Man)1 Publication
    Glycosylationi899 – 8991N-linked (GlcNAc...)1 Publication
    Glycosylationi957 – 9571N-linked (GlcNAc...)1 Publication
    Glycosylationi970 – 9701N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    The O-linked saccharide is not identified, but is probably mannose.1 Publication

    Keywords - PTMi

    Glycoprotein

    PTM databases

    UniCarbKBiP56526.

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00004308.

    Structurei

    3D structure databases

    ProteinModelPortaliP56526.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 2 hits.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P56526-1 [UniParc]FASTAAdd to Basket

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    MVKLTHLLAR AWLVPLAYGA SQSLLSTTAP SQPQFTIPAS ADVGAQLIAN    50
    IDDPQAADAQ SVCPGYKASK VQHNSRGFTA SLQLAGRPCN VYGTDVESLT 100
    LSVEYQDSDR LNIQILPTHV DSTNASWYFL SENLVPRPKA SLNASVSQSD 150
    LFVSWSNEPS FNFKVIRKAT GDALFSTEGT VLVYENQFIE FVTALPEEYN 200
    LYGLGEHITQ FRLQRNANLT IYPSDDGTPI DQNLYGQHPF YLDTRYYKGD 250
    RQNGSYIPVK SSEADASQDY ISLSHGVFLR NSHGLEILLR SQKLIWRTLG 300
    GGIDLTFYSG PAPADVTRQY LTSTVGLPAM QQYNTLGFHQ CRWGYNNWSD 350
    LADVVANFEK FEIPLEYIWT DIDYMHGYRN FDNDQHRFSY SEGDEFLSKL 400
    HESGRYYVPI VDAALYIPNP ENASDAYATY DRGAADDVFL KNPDGSLYIG 450
    AVWPGYTVFP DWHHPKAVDF WANELVIWSK KVAFDGVWYD MSEVSSFCVG 500
    SCGTGNLTLN PAHPSFLLPG EPGDIIYDYP EAFNITNATE AASASAGASS 550
    QAAATATTTS TSVSYLRTTP TPGVRNVEHP PYVINHDQEG HDLSVHAVSP 600
    NATHVDGVEE YDVHGLYGHQ GLNATYQGLL EVWSHKRRPF IIGRSTFAGS 650
    GKWAGHWGGD NYSKWWSMYY SISQALSFSL FGIPMFGADT CGFNGNSDEE 700
    LCNRWMQLSA FFPFYRNHNE LSTIPQEPYR WASVIEATKS AMRIRYAILP 750
    YFYTLFDLAH TTGSTVMRAL SWEFPNDPTL AAVETQFMVG PAIMVVPVLE 800
    PLVNTVKGVF PGVGHGEVWY DWYTQAAVDA KPGVNTTISA PLGHIPVYVR 850
    GGNILPMQEP ALTTREARQT PWALLAALGS NGTASGQLYL DDGESIYPNA 900
    TLHVDFTASR SSLRSSAQGR WKERNPLANV TVLGVNKEPS AVTLNGQAVF 950
    PGSVTYNSTS QVLFVGGLQN LTKGGAWAEN WVLEW 985
    Length:985
    Mass (Da):108,913
    Last modified:July 15, 1998 - v1
    Checksum:i9A18772AEB2E0927
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 282TT → LL in strain: GN-8.
    Natural varianti42 – 421D → A in strain: GN-8.
    Natural varianti929 – 9291N → M in strain: GN-8.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D45356 Genomic DNA. Translation: BAA23616.1.
    PIRiJC1199.
    JC1200.
    JC5561.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D45356 Genomic DNA. Translation: BAA23616.1 .
    PIRi JC1199.
    JC1200.
    JC5561.

    3D structure databases

    ProteinModelPortali P56526.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00004308.

    Chemistry

    ChEMBLi CHEMBL3435.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.
    mycoCLAPi AGL31A_ASPNG.

    PTM databases

    UniCarbKBi P56526.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1501.

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 2 hits.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of an alpha-glucosidase gene from Aspergillus niger and its expression in A. nidulans."
      Nakamura A., Nishimura I., Yokoyama A., Lee D.-G., Hidaka M., Masaki H., Kimura A., Chiba S., Uozumi T.
      J. Biotechnol. 53:75-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GN-3.
    2. "Complete amino acid sequence of crystalline alpha-glucosidase from Aspergillus niger."
      Kimura A., Takata M., Sakai O., Matsui H., Takai N., Takayanagi T., Nishimua I., Uozumi T., Chiba S.
      Biosci. Biotechnol. Biochem. 56:1368-1370(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-252 AND 267-985, GLYCOSYLATION AT THR-36; ASN-124; ASN-143; ASN-218; ASN-347; ASN-422; ASN-506; ASN-534; SER-545; SER-550; THR-559; SER-560; THR-561; SER-562; THR-571; ASN-601; ASN-623; ASN-835; ASN-881; SER-895; ASN-899; ASN-957 AND ASN-970.
      Strain: GN-8.

    Entry informationi

    Entry nameiAGLU_ASPNG
    AccessioniPrimary (citable) accession number: P56526
    Secondary accession number(s): O13451
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3