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Q09840

- AMY2_SCHPO

UniProt

Q09840 - AMY2_SCHPO

Protein

Alpha-amylase 2

Gene

aah2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

    Cofactori

    Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091SubstrateBy similarity
    Metal bindingi147 – 1471Calcium 1By similarity
    Metal bindingi202 – 2021Calcium 1By similarity
    Binding sitei231 – 2311SubstrateBy similarity
    Active sitei233 – 2331NucleophileBy similarity
    Metal bindingi233 – 2331Calcium 2By similarity
    Metal bindingi237 – 2371Calcium 1; via carbonyl oxygenBy similarity
    Active sitei257 – 2571Proton donorBy similarity
    Metal bindingi257 – 2571Calcium 2By similarity
    Binding sitei261 – 2611Substrate; via amide nitrogenBy similarity
    Binding sitei324 – 3241SubstrateBy similarity
    Sitei325 – 3251Transition state stabilizerBy similarity
    Binding sitei372 – 3721SubstrateBy similarity

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. calcium ion binding Source: InterPro

    GO - Biological processi

    1. cellular polysaccharide catabolic process Source: PomBase
    2. extracellular polysaccharide metabolic process Source: PomBase
    3. fungal-type cell wall biogenesis Source: PomBase
    4. regulation of cell shape Source: PomBase

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase 2 (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    Gene namesi
    Name:aah2
    ORF Names:SPAC23D3.14c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC23D3.14c.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: PomBase
    2. endoplasmic reticulum Source: PomBase

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 551527Alpha-amylase 2PRO_0000001355Add
    BLAST
    Propeptidei552 – 58130Removed in mature formSequence AnalysisPRO_0000255452Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 64By similarity
    Disulfide bondi176 ↔ 191By similarity
    Disulfide bondi267 ↔ 311By similarity
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
    Lipidationi551 – 5511GPI-anchor amidated serineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4695620.
    STRINGi4896.SPAC23D3.14c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ09840.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni236 – 2372Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000165530.
    KOiK01176.
    OMAiCWIDYSN.
    OrthoDBiEOG7RBZJ4.
    PhylomeDBiQ09840.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR013777. A-amylase_fun.
    IPR015340. A_amylase_DUF1966_C.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF09260. DUF1966. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q09840-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYRRNICLR IGWMLLFAFI PAYAGHSAEE WKRRSIYQII TDRFSLEEGA    50
    TERIPCDPVR FMYCGGTWNG IRNHLDYIQG MGFDAIWISP IFENVEGNDI 100
    DGSSYHGYWT TNLYELNHHF GTKEEFMELI QELHKRDIWI LLDVAINSMA 150
    INGPLEQMSF EKVIPFNDAS FFHPHCWVDY ESNDIESVQN CWLGDENLLL 200
    ADVDTENEVV LSVLEKWIKN VVQEYDIDGI RFDAIKHAPI EFWLRMSKAA 250
    DIFTIGEYFT GSPAEACDYQ NSGLDSFLNF PLYWPITWAF NNTGLQCEAL 300
    AIAINQINEE CNDINVLGTF IGNHDLPRIS HNNTDQARIM NAITFVMMWD 350
    GIPIIYYGTE QNFNSYHDPF NREALWLSNF DMENVYYKLI GILNRFRKSV 400
    QRQEENYVNT RSTILSVKIH HIVVQKLNVI TVLNNYGIHN EERLSIVFKP 450
    LGASPKDTFF DIINNQKYVV NTDGTLKVVI TNGFPIVLYP TSKIETSLPQ 500
    FTATLLPEIT FVPSITVTTH YVLPTLLAPL GYDIREHPGG QQFWNTLTAK 550
    SEAKTIRSFT KLKLFILLIA VPFALPMIIL I 581
    Length:581
    Mass (Da):67,005
    Last modified:February 1, 1996 - v1
    Checksum:iFE9DE99D323E1890
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA91249.1.
    PIRiT38289. S62505.
    RefSeqiNP_594551.1. NM_001019980.1.

    Genome annotation databases

    EnsemblFungiiSPAC23D3.14c.1; SPAC23D3.14c.1:pep; SPAC23D3.14c.
    GeneIDi2541501.
    KEGGispo:SPAC23D3.14c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA91249.1 .
    PIRi T38289. S62505.
    RefSeqi NP_594551.1. NM_001019980.1.

    3D structure databases

    ProteinModelPortali Q09840.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4695620.
    STRINGi 4896.SPAC23D3.14c-1.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC23D3.14c.1 ; SPAC23D3.14c.1:pep ; SPAC23D3.14c .
    GeneIDi 2541501.
    KEGGi spo:SPAC23D3.14c.

    Organism-specific databases

    PomBasei SPAC23D3.14c.

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000165530.
    KOi K01176.
    OMAi CWIDYSN.
    OrthoDBi EOG7RBZJ4.
    PhylomeDBi Q09840.

    Miscellaneous databases

    NextBioi 20802600.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR013777. A-amylase_fun.
    IPR015340. A_amylase_DUF1966_C.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF09260. DUF1966. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001024. Alph-amyl_fung. 1 hit.
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "Genome-wide identification of fungal GPI proteins."
      De Groot P.W., Hellingwerf K.J., Klis F.M.
      Yeast 20:781-796(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PREDICTION OF GPI-ANCHOR.
    3. "An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in Schizosaccharomyces pombe."
      Morita T., Tanaka N., Hosomi A., Giga-Hama Y., Takegawa K.
      Biosci. Biotechnol. Biochem. 70:1454-1463(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE NAME.
    4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMY2_SCHPO
    AccessioniPrimary (citable) accession number: Q09840
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 114 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

    Complete proteome, 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