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O04893

- AGLU_SPIOL

UniProt

O04893 - AGLU_SPIOL

Protein

Alpha-glucosidase

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Alpha-glucosidase I and II have high activity towards malto-oligosaccharides and starch, while form III and IV have high activity towards malto-oligosaccharides but low activity toward 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 sitei465 – 4651By similarity
    Active sitei468 – 4681By similarity
    Active sitei564 – 5641Proton 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Maltase
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 903879Alpha-glucosidasePRO_0000018584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi600 – 6001N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Four different forms (I-IV) may be produced by post-translational modification.

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliO04893.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.70. 2 hits.
    InterProiIPR013785. Aldolase_TIM.
    IPR011013. 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.

    O04893-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKKIPSLAL GILLVFLLQY LVAGISTSEN DPEGVIGYGY KVKSVKVDSG    50
    TRRSLTALPQ LVKNSSVYGP DIQLLSITAS LESNDRLRVR ITDAKHRRWE 100
    IPDNILHRHQ PPPPPPHSLS SLYRTLLSSP TTNRRKILLS HPNSDLTFSL 150
    INTTPFGFTI SRKSTHDVLF DATPDPTNPN TFLIFIDQYL HLTSSLPGTR 200
    AHIYGLGEHS KPTFQLAHNQ TLTMRAADIP SSNPDVNLYG SHPFYMDVRS 250
    SPVAGSTHGV LLLNSNGMDV EYTGNRITYK VIGGIIDLYF FAGPSPGQVV 300
    EQFTRVIGRP APMPYWAFGF QQCRYGYHDV YELQSVVAGY AKAKIPLEVM 350
    WTDIDYMDAY KDFTLDPVNF PLDKMKKFVN NLHKNGQKYV VILDPGISTN 400
    KTYETYIRGM KHDVFLKRNG KPYLGSVWPG PVYFPDFLKP SALTFWTDEI 450
    KRFLNLLPVD GLWIDMNEIS NFISSPPIPG STLDNPPYKI NNSGVMLPII 500
    NKTIPPTAMH YGDIPEYNVH NLFGYLEARV TRAALIKLTE KRPFVLSRST 550
    FSGSGKYTAH WTGDNAATWN DLVYSIPSML DFGLFGIPMV GADICGFLGN 600
    TTEELCRRWI QLGAFYPFSR DHSSLGTTYQ ELYRWESVAA SARKVLGLRY 650
    TLLPYFYTLM YEAQLNGIPI ARPLFFSFPD DIKTYGISSQ FLLGKGVMVS 700
    PVLKPGVVSV TAYFPRGNWF DLFDYTRSVT ASTGRYVTLS APPDHINVHI 750
    QEGNILAMQG KAMTTQAARK TPFHLLVVMS DCGASFGELF LDDGVEVTMG 800
    VNRGKWTFVK FIAASAKQTC IITSDVVSGE FAVSQKWVID KVTILGLRKG 850
    TKINGYTVRT GAVTRKGDKS KLKSTPDRKG EFIVAEISGL NLLLGREFKL 900
    VLH 903
    Length:903
    Mass (Da):100,881
    Last modified:July 1, 1997 - v1
    Checksum:i5B054E27C20EC33A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86624 mRNA. Translation: BAA19924.1.
    PIRiT09143.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86624 mRNA. Translation: BAA19924.1 .
    PIRi T09143.

    3D structure databases

    ProteinModelPortali O04893.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.70. 2 hits.
    InterProi IPR013785. Aldolase_TIM.
    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. "Molecular cloning and characterization of a cDNA encoding alpha-glucosidase from spinach."
      Sugimoto M., Furui S., Suzuki Y.
      Plant Mol. Biol. 33:765-768(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: cv. Dash.

    Entry informationi

    Entry nameiAGLU_SPIOL
    AccessioniPrimary (citable) accession number: O04893
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 62 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