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P53051

- MALX3_YEAST

UniProt

P53051 - MALX3_YEAST

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Protein
Oligo-1,6-glucosidase IMA1
Gene
IMA1, YGR287C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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
Complete GO annotation...

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 IMA1
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP53051.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti428 – 4281E → D in BAD00094. 1 Publication

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...

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 113 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.

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

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