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P53051 (MALX3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oligo-1,6-glucosidase IMA1

EC=3.2.1.10
Alternative name(s):
Alpha-glucosidase
Isomaltase 1
Gene names
Name:IMA1
Ordered Locus Names:YGR287C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.9

Catalytic activity

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

Subcellular location

Mitochondrion Ref.6 Ref.8.

Induction

Expression is increased in response to the addition of maltose, isomaltose, and alpha-methylglucopyranoside. Ref.9

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399402EBI-10464,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 589588Oligo-1,6-glucosidase IMA1
PRO_0000054333

Sites

Active site2151Nucleophile
Active site2771Proton donor
Site3521Transition state stabilizer

Experimental info

Mutagenesis2151D → A: Abolishes catalytic activity. Ref.1
Mutagenesis2161V → T: Can also hydrolyze maltose. Ref.1
Mutagenesis2171G → A: Does not alter substrate specificity. Ref.1
Mutagenesis2181S → G: Does not alter substrate specificity. Ref.1
Sequence conflict4281E → D in BAD00094. Ref.1

Secondary structure

................................................................................................................. 589
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53051 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 08869180588053B6

FASTA58968,592
        10         20         30         40         50         60 
MTISSAHPET EPKWWKEATF YQIYPASFKD SNDDGWGDMK GIASKLEYIK ELGADAIWIS 

        70         80         90        100        110        120 
PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL GMKFITDLVI NHCSSEHEWF 

       130        140        150        160        170        180 
KESRSSKTNP KRDWFFWRPP KGYDAEGKPI PPNNWKSYFG GSAWTFDEKT QEFYLRLFCS 

       190        200        210        220        230        240 
TQPDLNWENE DCRKAIYESA VGYWLDHGVD GFRIDVGSLY SKVVGLPDAP VVDKNSTWQS 

       250        260        270        280        290        300 
SDPYTLNGPR IHEFHQEMNQ FIRNRVKDGR EIMTVGEMQH ASDETKRLYT SASRHELSEL 

       310        320        330        340        350        360 
FNFSHTDVGT SPLFRYNLVP FELKDWKIAL AELFRYINGT DCWSTIYLEN HDQPRSITRF 

       370        380        390        400        410        420 
GDDSPKNRVI SGKLLSVLLS ALTGTLYVYQ GQELGQINFK NWPVEKYEDV EIRNNYNAIK 

       430        440        450        460        470        480 
EEHGENSEEM KKFLEAIALI SRDHARTPMQ WSREEPNAGF SGPSAKPWFY LNDSFREGIN 

       490        500        510        520        530        540 
VEDEIKDPNS VLNFWKEALK FRKAHKDITV YGYDFEFIDL DNKKLFSFTK KYNNKTLFAA 

       550        560        570        580 
LNFSSDATDF KIPNDDSSFK LEFGNYPKKE VDASSRTLKP WEGRIYISE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS59370.
RefSeqNP_011803.3. NM_001181416.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A47X-ray1.59A1-589[»]
3A4AX-ray1.60A1-589[»]
3AJ7X-ray1.30A1-589[»]
3AXHX-ray1.80A1-589[»]
3AXIX-ray1.40A1-589[»]
ProteinModelPortalP53051.
SMRP53051. Positions 4-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33537. 36 interactions.
IntActP53051. 5 interactions.
MINTMINT-4083809.
STRING4932.YGR287C.

Chemistry

BindingDBP53051.
ChEMBLCHEMBL5848.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.
mycoCLAPOGL13A_YEAST.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR287C; YGR287C; YGR287C.
GeneID853204.
KEGGsce:YGR287C.

Organism-specific databases

CYGDYGR287c.
SGDS000003519. IMA1.

Phylogenomic databases

GeneTreeENSGT00530000063127.
HOGENOMHOG000220641.
KOK01187.
OMANGARIHE.
OrthoDBEOG7M3J7X.

Enzyme and pathway databases

BioCycYEAST:YGR287C-MONOMER.

Gene expression databases

ArrayExpressP53051.
GenevestigatorP53051.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP53051.
NextBio973383.

Entry information

Entry nameMALX3_YEAST
AccessionPrimary (citable) accession number: P53051
Secondary accession number(s): D6VV64, Q76CZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries