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O04931

- AGLU_BETVU

UniProt

O04931 - AGLU_BETVU

Protein

Alpha-glucosidase

Gene
N/A
Organism
Beta vulgaris (Sugar beet)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    High activity for alpha-glucan.

    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 sitei469 – 46911 Publication
    Active sitei472 – 4721By similarity
    Active sitei568 – 5681Proton donorBy similarity

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: UniProtKB
    2. carbohydrate binding Source: InterPro
    3. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Maltase
    OrganismiBeta vulgaris (Sugar beet)
    Taxonomic identifieri161934 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeBeta

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 913885Alpha-glucosidasePRO_0000018582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi823 – 8231N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Glycoprotein

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    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.

    O04931-1 [UniParc]FASTAAdd to Basket

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    MERSKLPRYI CPTLAVVLPL VLCMVVEGAT TSKNDNQGEA IGYGYQVKNA    50
    KVDNSTGKSL TALLQLIRNS PVYGPDIHFL SFTASFEEDD TLRIRFTDAN 100
    NRRWEIPNEV LPRPPPPPSP PPLSSLQHLP KPIPQNQPTT TVLSHPHSDL 150
    AFTLFHTTPF GFTIYRKSTH DVLFDATPIP SNPTTFLIYK DQYLQLSSSL 200
    PAQQAHLYGL GEHTKPTFQL AHNQILTLWN ADIASFNRDL NLYGSHPFYM 250
    DVRSSPMVGS THGVFLLNSN GMDVEYTGDR ITYKVIGGII DLYIFAGRTP 300
    EMVLDQYTKL IGRPAPMPYW AFGFHQCRWG YRDVNEIETV VDKYAEARIP 350
    LEVMWTDIDY MDAFKDFTLD PVHFPLDKMQ QFVTKLHRNG QRYVPILDPG 400
    INTNKSYGTF IRGMQSNVFI KRNGNPYLGS VWPGPVYYPD FLDPAARSFW 450
    VDEIKRFRDI LPIDGIWIDM NEASNFITSA PTPGSTLDNP PYKINNSGGR 500
    VPINSKTIPA TAMHYGNVTE YNAHNLYGFL ESQATREALV RPATRGPFLL 550
    SRSTFAGSGK YTAHWTGDNA ARWDDLQYSI PTMLNFGLFG MPMIGADICG 600
    FAESTTEELC CRWIQLGAFY PFSRDHSARD TTHQELYLWE SVAASARTVL 650
    GLRYELLPYY YTLMYDANLR GSPIARPLSF TFPDDVATYG ISSQFLIGRG 700
    IMVSPVLQPG SSIVNAYSPR GNWVSLSNYT SSVSVSAGTY VSLSAPPDHI 750
    NVHIHEGNIV AMQGEAMTTQ AARSTPFHLL VVMSDHVAST GELFLDNGIE 800
    MDIGGPGGKW TLVRFFAESG INNLTISSEV VNRGYAMSQR WVMDKITILG 850
    LKRRVKIKEY TVQKDAGAIK VKGLGRRTSS HNQGGFFVSV ISDLRQLVGQ 900
    AFKLELEFEG ATR 913
    Length:913
    Mass (Da):102,117
    Last modified:July 1, 1997 - v1
    Checksum:i02AC4F0B505369CC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89615 mRNA. Translation: BAA20343.1.
    PIRiJC5463.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89615 mRNA. Translation: BAA20343.1 .
    PIRi JC5463.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL4348.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    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 a cDNA encoding alpha-glucosidase from sugar beet."
      Matsui H., Iwanami S., Ito H., Mori H., Honma M., Chiba S.
      Biosci. Biotechnol. Biochem. 61:875-880(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: cv. NK-152.
    2. "Chemical modification and amino acid sequence of active site in sugar beet alpha-glucosidase."
      Iwanami S., Matsui H., Kimura A., Ito H., Mori H., Honma M., Chiba S.
      Biosci. Biotechnol. Biochem. 59:459-463(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 464-472.

    Entry informationi

    Entry nameiAGLU_BETVU
    AccessioniPrimary (citable) accession number: O04931
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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