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P53051

- MALX3_YEAST

UniProt

P53051 - MALX3_YEAST

Protein

Oligo-1,6-glucosidase IMA1

Gene

IMA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.2 Publications

    Catalytic activityi

    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei215 – 2151Nucleophile
    Active sitei277 – 2771Proton donor
    Sitei352 – 3521Transition state stabilizer

    GO - Molecular functioni

    1. cation binding Source: InterPro
    2. oligo-1,6-glucosidase activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. disaccharide catabolic process Source: SGD
    2. maltose metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Maltose metabolism

    Enzyme and pathway databases

    BioCyciYEAST:YGR287C-MONOMER.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.
    mycoCLAPiOGL13A_YEAST.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oligo-1,6-glucosidase IMA1 (EC:3.2.1.10)
    Alternative name(s):
    Alpha-glucosidase
    Isomaltase 1
    Gene namesi
    Name:IMA1
    Ordered Locus Names:YGR287C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR287c.
    SGDiS000003519. IMA1.

    Subcellular locationi

    Mitochondrion 2 Publications

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi215 – 2151D → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi216 – 2161V → T: Can also hydrolyze maltose. 1 Publication
    Mutagenesisi217 – 2171G → A: Does not alter substrate specificity. 1 Publication
    Mutagenesisi218 – 2181S → G: Does not alter substrate specificity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 589588Oligo-1,6-glucosidase IMA1PRO_0000054333Add
    BLAST

    Proteomic databases

    MaxQBiP53051.

    Expressioni

    Inductioni

    Expression is increased in response to the addition of maltose, isomaltose, and alpha-methylglucopyranoside.1 Publication

    Gene expression databases

    GenevestigatoriP53051.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399402EBI-10464,EBI-16219

    Protein-protein interaction databases

    BioGridi33537. 36 interactions.
    IntActiP53051. 5 interactions.
    MINTiMINT-4083809.
    STRINGi4932.YGR287C.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103
    Helixi14 – 174
    Beta strandi20 – 234
    Helixi25 – 273
    Beta strandi31 – 366
    Helixi39 – 446
    Helixi46 – 527
    Beta strandi55 – 595
    Turni68 – 714
    Beta strandi75 – 806
    Turni82 – 843
    Helixi87 – 9913
    Beta strandi103 – 1086
    Helixi118 – 1236
    Beta strandi127 – 1293
    Helixi132 – 1343
    Beta strandi141 – 1433
    Beta strandi160 – 1678
    Turni168 – 1714
    Beta strandi172 – 1754
    Beta strandi177 – 1793
    Helixi190 – 20011
    Helixi202 – 2065
    Beta strandi211 – 2144
    Helixi217 – 2193
    Beta strandi237 – 2393
    Helixi242 – 2454
    Helixi251 – 26515
    Beta strandi273 – 2797
    Helixi283 – 2908
    Helixi292 – 2943
    Beta strandi298 – 3025
    Helixi304 – 3074
    Beta strandi314 – 3185
    Helixi323 – 3319
    Turni332 – 3343
    Helixi335 – 3373
    Helixi356 – 3605
    Turni365 – 3673
    Helixi368 – 38013
    Beta strandi382 – 3898
    Helixi392 – 3943
    Helixi404 – 4063
    Helixi410 – 42314
    Beta strandi425 – 4273
    Helixi428 – 44013
    Helixi442 – 4454
    Turni455 – 4595
    Helixi473 – 4775
    Helixi481 – 4866
    Helixi491 – 50414
    Helixi506 – 5094
    Beta strandi513 – 5197
    Beta strandi523 – 53210
    Beta strandi535 – 5428
    Beta strandi544 – 5463
    Beta strandi559 – 5668
    Turni568 – 5703
    Beta strandi583 – 5886

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A47X-ray1.59A1-589[»]
    3A4AX-ray1.60A1-589[»]
    3AJ7X-ray1.30A1-589[»]
    3AXHX-ray1.80A1-589[»]
    3AXIX-ray1.40A1-589[»]
    ProteinModelPortaliP53051.
    SMRiP53051. Positions 4-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53051.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00530000063127.
    HOGENOMiHOG000220641.
    KOiK01187.
    OMAiVEPYRDY.
    OrthoDBiEOG7M3J7X.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR015902. 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.
    [Graphical view]
    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.

    P53051-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTISSAHPET EPKWWKEATF YQIYPASFKD SNDDGWGDMK GIASKLEYIK    50
    ELGADAIWIS PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL 100
    GMKFITDLVI NHCSSEHEWF KESRSSKTNP KRDWFFWRPP KGYDAEGKPI 150
    PPNNWKSYFG GSAWTFDEKT QEFYLRLFCS TQPDLNWENE DCRKAIYESA 200
    VGYWLDHGVD GFRIDVGSLY SKVVGLPDAP VVDKNSTWQS SDPYTLNGPR 250
    IHEFHQEMNQ FIRNRVKDGR EIMTVGEMQH ASDETKRLYT SASRHELSEL 300
    FNFSHTDVGT SPLFRYNLVP FELKDWKIAL AELFRYINGT DCWSTIYLEN 350
    HDQPRSITRF GDDSPKNRVI SGKLLSVLLS ALTGTLYVYQ GQELGQINFK 400
    NWPVEKYEDV EIRNNYNAIK EEHGENSEEM KKFLEAIALI SRDHARTPMQ 450
    WSREEPNAGF SGPSAKPWFY LNDSFREGIN VEDEIKDPNS VLNFWKEALK 500
    FRKAHKDITV YGYDFEFIDL DNKKLFSFTK KYNNKTLFAA LNFSSDATDF 550
    KIPNDDSSFK LEFGNYPKKE VDASSRTLKP WEGRIYISE 589
    Length:589
    Mass (Da):68,592
    Last modified:October 1, 1996 - v1
    Checksum:i08869180588053B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti428 – 4281E → D in BAD00094. (PubMed:15291818)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB109221 mRNA. Translation: BAD00094.1.
    D43761 Genomic DNA. Translation: BAA07818.1.
    Z73072 Genomic DNA. Translation: CAA97319.1.
    Z73073 Genomic DNA. Translation: CAA97321.1.
    BK006941 Genomic DNA. Translation: DAA08375.1.
    PIRiS59370.
    RefSeqiNP_011803.3. NM_001181416.3.

    Genome annotation databases

    EnsemblFungiiYGR287C; YGR287C; YGR287C.
    GeneIDi853204.
    KEGGisce:YGR287C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB109221 mRNA. Translation: BAD00094.1 .
    D43761 Genomic DNA. Translation: BAA07818.1 .
    Z73072 Genomic DNA. Translation: CAA97319.1 .
    Z73073 Genomic DNA. Translation: CAA97321.1 .
    BK006941 Genomic DNA. Translation: DAA08375.1 .
    PIRi S59370.
    RefSeqi NP_011803.3. NM_001181416.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A47 X-ray 1.59 A 1-589 [» ]
    3A4A X-ray 1.60 A 1-589 [» ]
    3AJ7 X-ray 1.30 A 1-589 [» ]
    3AXH X-ray 1.80 A 1-589 [» ]
    3AXI X-ray 1.40 A 1-589 [» ]
    ProteinModelPortali P53051.
    SMRi P53051. Positions 4-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33537. 36 interactions.
    IntActi P53051. 5 interactions.
    MINTi MINT-4083809.
    STRINGi 4932.YGR287C.

    Chemistry

    BindingDBi P53051.
    ChEMBLi CHEMBL5848.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.
    mycoCLAPi OGL13A_YEAST.

    Proteomic databases

    MaxQBi P53051.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR287C ; YGR287C ; YGR287C .
    GeneIDi 853204.
    KEGGi sce:YGR287C.

    Organism-specific databases

    CYGDi YGR287c.
    SGDi S000003519. IMA1.

    Phylogenomic databases

    GeneTreei ENSGT00530000063127.
    HOGENOMi HOG000220641.
    KOi K01187.
    OMAi VEPYRDY.
    OrthoDBi EOG7M3J7X.

    Enzyme and pathway databases

    BioCyci YEAST:YGR287C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P53051.
    NextBioi 973383.

    Gene expression databases

    Genevestigatori P53051.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProi 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.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae."
      Yamamoto K., Nakayama A., Yamamoto Y., Tabata S.
      Eur. J. Biochem. 271:3414-3420(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-13; 161-169; 247-258; 288-294; 314-320 AND 577-584, FUNCTION, MUTAGENESIS OF ASP-215; VAL-216; GLY-217 AND SER-218.
      Strain: ATCC 56960 / D-346.
    2. Tonouchi A.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2 genes and an ABC transporter gene."
      Volckaert G., Voet M., Robben J.
      Yeast 13:251-259(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
      Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
      J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. "Characterization of a new multigene family encoding isomaltases in the yeast Saccharomyces cerevisiae, the IMA family."
      Teste M.A., Francois J.M., Parrou J.L.
      J. Biol. Chem. 285:26815-26824(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    10. "Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose."
      Yamamoto K., Miyake H., Kusunoki M., Osaki S.
      FEBS J. 277:4205-4214(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MALTOSE.

    Entry informationi

    Entry nameiMALX3_YEAST
    AccessioniPrimary (citable) accession number: P53051
    Secondary accession number(s): D6VV64, Q76CZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 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

    Miscellaneous

    Present with 752 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3