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P53051

- MALX3_YEAST

UniProt

P53051 - MALX3_YEAST

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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

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. sucrose alpha-glucosidase activity Source: SGD

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.
ReactomeiREACT_243973. Amino acid transport across the plasma membrane.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP53051.
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

        10         20         30         40         50
MTISSAHPET EPKWWKEATF YQIYPASFKD SNDDGWGDMK GIASKLEYIK
60 70 80 90 100
ELGADAIWIS PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL
110 120 130 140 150
GMKFITDLVI NHCSSEHEWF KESRSSKTNP KRDWFFWRPP KGYDAEGKPI
160 170 180 190 200
PPNNWKSYFG GSAWTFDEKT QEFYLRLFCS TQPDLNWENE DCRKAIYESA
210 220 230 240 250
VGYWLDHGVD GFRIDVGSLY SKVVGLPDAP VVDKNSTWQS SDPYTLNGPR
260 270 280 290 300
IHEFHQEMNQ FIRNRVKDGR EIMTVGEMQH ASDETKRLYT SASRHELSEL
310 320 330 340 350
FNFSHTDVGT SPLFRYNLVP FELKDWKIAL AELFRYINGT DCWSTIYLEN
360 370 380 390 400
HDQPRSITRF GDDSPKNRVI SGKLLSVLLS ALTGTLYVYQ GQELGQINFK
410 420 430 440 450
NWPVEKYEDV EIRNNYNAIK EEHGENSEEM KKFLEAIALI SRDHARTPMQ
460 470 480 490 500
WSREEPNAGF SGPSAKPWFY LNDSFREGIN VEDEIKDPNS VLNFWKEALK
510 520 530 540 550
FRKAHKDITV YGYDFEFIDL DNKKLFSFTK KYNNKTLFAA LNFSSDATDF
560 570 580
KIPNDDSSFK LEFGNYPKKE VDASSRTLKP WEGRIYISE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P53051.
KOi K01187.
OMAi VEPYRDY.
OrthoDBi EOG7M3J7X.

Enzyme and pathway databases

BioCyci YEAST:YGR287C-MONOMER.
Reactomei REACT_243973. Amino acid transport across the plasma membrane.

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: November 26, 2014
This is version 116 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