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Q9C0Y4

- AGLU_SCHPO

UniProt

Q9C0Y4 - AGLU_SCHPO

Protein

Alpha-glucosidase

Gene

agl1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (29 Aug 2001)
      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 sitei481 – 4811Nucleophile
    Active sitei484 – 4841
    Active sitei647 – 6471Proton donor

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: PomBase
    2. carbohydrate binding Source: InterPro
    3. maltose alpha-glucosidase activity Source: PomBase
    4. starch alpha-glucosidase activity Source: PomBase

    GO - Biological processi

    1. cellular polysaccharide catabolic process Source: PomBase
    2. maltose catabolic process Source: PomBase

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.
    mycoCLAPiAGL31A_SCHPO.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Maltase
    Gene namesi
    Name:agl1
    Synonyms:agl
    ORF Names:SPAPB24D3.10c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAPB24D3.10c.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: PomBase

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi218 – 2181D → N: Almost total loss of activity. 1 Publication
    Mutagenesisi287 – 2871D → N: No loss of activity. 1 Publication
    Mutagenesisi355 – 3551D → E or N: Almost total loss of activity. 1 Publication
    Mutagenesisi481 – 4811D → A, E or N: Loss of activity. 1 Publication
    Mutagenesisi484 – 4841E → A or Q: Loss of activity. 1 Publication
    Mutagenesisi484 – 4841E → D: No loss of activity. 1 Publication
    Mutagenesisi647 – 6471D → A, E or N: Loss of activity. 1 Publication
    Mutagenesisi676 – 6761D → N: No loss of activity. 1 Publication
    Mutagenesisi714 – 7141E → Q: No loss of activity. 1 Publication
    Mutagenesisi877 – 8771D → N: Almost total loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 969945Alpha-glucosidasePRO_0000018581Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi589 – 5891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi648 – 6481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi821 – 8211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi915 – 9151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi934 – 9341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi954 – 9541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi966 – 9661N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9C0Y4.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4702058.
    STRINGi4896.SPAPB24D3.10c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C0Y4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000041175.
    OrthoDBiEOG77T1CZ.
    PhylomeDBiQ9C0Y4.

    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. 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.

    Q9C0Y4-1 [UniParc]FASTAAdd to Basket

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    MMISTAYQSL FLTALFSAIS IAVGNVYQTL NVIGDRNVTI PTNGIPQRLS    50
    VYDPYRGVNC QGYQAVNISE SQNGVTAYLA LLGEPCYAYG TDYPLLFLNV 100
    TYEEADRVHI SIKDANNTQF QFTSRKDLWD APLYSPSYNN TNLLYNFSYN 150
    ANPFEFWVTR KSDGEVLFDT RGQKLVFEDQ YIELTTNMVE NYNLYGLAET 200
    IHGLRLGNNL TRTFWANDEP SPVDQNMYGS HPYYLEQRYK ADGINSTLNE 250
    TTYTSSSHGV LMLTANGMDV LLRQDYLQYR MIGGVIDLFV YSGSTESPKE 300
    TVKQFVQSIG KPAMHQYWTL GYHSCRWGYT NITEIMDVRQ NYIDADIPVE 350
    TFWSDIDYME KYRDFTVDPV SYSKSDMQTF FSDLVSNHQH YVPIIDAAIY 400
    AANPYNHTDD SYYPYYAGVE KDIFLKNPNG SIYIGAVWPG FTAFPDFTNP 450
    DVVDYWKDCL INLTYAFGSN GTVPFSGIWT DMNEPSSFCV GSCGSAMIDL 500
    NPAEPLTGIS KQYSIPEGFN VSNVTEYSSA YSASLSNYYA TATSSVFQIV 550
    SPTATPLGLK PDYNIDWPPY AINNEQGNHD IANHIVSPNA TTHDGTQRYD 600
    IFNMYGYGET KVSYAALTQI SPNERPFILS RSTFLGSGVY GAHWLGDNHS 650
    LWSNMFFSIS GMIVFNMMGI PMVGADVCGF LGDSDEELCS RWMAMGAFSP 700
    FYRNHNNIYQ ISQEPYTWSS VAEASRRAMY IRYSLLPYWY TIMAKASQDG 750
    TPALRALFVE FPNDPTLADV DRQFMVGDSL LVTPVLEPNV EYVQGVFPGD 800
    NSTVWYDWYN HTEIVRQYNE NVTLYAPLEH INVAIRGGSV LPMQQPSLTT 850
    YESRQNPFNL LVALDRDGSA TGELYLDDGV SIELNATLSV SFTFSDGVLS 900
    AVPTGSYEVS QPLANVTILG LTESPSSITL NGQNVSSFQY SNDTEELLIT 950
    GLQNITSSGA FANSWNLTL 969
    Length:969
    Mass (Da):108,686
    Last modified:August 29, 2001 - v2
    Checksum:iF3122E2CFA551C25
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301L → F in CAC36906. (PubMed:11859360)Curated
    Sequence conflicti220 – 2201P → A in BAB43946. (PubMed:11298744)Curated
    Sequence conflicti507 – 5071T → V in BAB43946. (PubMed:11298744)Curated
    Sequence conflicti566 – 5661D → N in BAB43946. (PubMed:11298744)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAC36906.1.
    AB045751 mRNA. Translation: BAB43946.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAC36906.1 .
    AB045751 mRNA. Translation: BAB43946.1 .

    3D structure databases

    ProteinModelPortali Q9C0Y4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4702058.
    STRINGi 4896.SPAPB24D3.10c-1.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.
    mycoCLAPi AGL31A_SCHPO.

    Proteomic databases

    MaxQBi Q9C0Y4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    PomBasei SPAPB24D3.10c.

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000041175.
    OrthoDBi EOG77T1CZ.
    PhylomeDBi Q9C0Y4.

    Miscellaneous databases

    NextBioi 20804509.

    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. 1 hit.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of alpha-glucosidase from Schizosaccharomyces pombe."
      Okuyama M., Okuno A., Shimizu N., Mori H., Kimura A., Chiba S.
      Eur. J. Biochem. 268:2270-2280(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36; 175-194; 375-395 AND 427-451, MUTAGENESIS OF ASP-218; ASP-287; ASP-355; ASP-481; GLU-484; ASP-647; ASP-676; GLU-714 AND ASP-877.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiAGLU_SCHPO
    AccessioniPrimary (citable) accession number: Q9C0Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3