P53051 (MALX3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Maltose metabolism
Cellular component	Mitochondrion
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	disaccharide catabolic process Inferred from mutant phenotype Ref.9. Source: SGD maltose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from direct assay Ref.6Ref.8. Source: SGD
Molecular_function	cation binding Inferred from electronic annotation. Source: InterPro oligo-1,6-glucosidase activity Inferred from direct assay Ref.1PubMed 20471265. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RSP5	P39940	2	EBI-10464,EBI-16219

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 589

588

Oligo-1,6-glucosidase IMA1

PRO_0000054333

Sites

Active site

215

1

Nucleophile

Active site

277

1

Proton donor

Site

352

1

Transition state stabilizer

Experimental info

Mutagenesis

215

1

D → A: Abolishes catalytic activity. Ref.1

Mutagenesis

216

1

V → T: Can also hydrolyze maltose. Ref.1

Mutagenesis

217

1

G → A: Does not alter substrate specificity. Ref.1

Mutagenesis

218

1

S → G: Does not alter substrate specificity. Ref.1

Sequence conflict

428

1

E → D in BAD00094. Ref.1

Secondary structure

1

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589

Helix Strand Turn

Details...

Helix

8 – 10

3

Helix

14 – 17

4

Beta strand

20 – 23

4

Helix

25 – 27

3

Beta strand

31 – 36

6

Helix

39 – 44

6

Helix

46 – 52

7

Beta strand

55 – 59

5

Turn

68 – 71

4

Beta strand

75 – 80

6

Turn

82 – 84

3

Helix

87 – 99

13

Beta strand

103 – 108

6

Helix

118 – 123

6

Beta strand

127 – 129

3

Helix

132 – 134

3

Beta strand

141 – 143

3

Beta strand

160 – 167

8

Turn

168 – 171

4

Beta strand

172 – 175

4

Beta strand

177 – 179

3

Helix

190 – 200

11

Helix

202 – 206

5

Beta strand

211 – 214

4

Helix

217 – 219

3

Beta strand

237 – 239

3

Helix

242 – 245

4

Helix

251 – 265

15

Beta strand

273 – 279

7

Helix

283 – 290

8

Helix

292 – 294

3

Beta strand

298 – 302

5

Helix

304 – 307

4

Beta strand

314 – 318

5

Helix

323 – 331

9

Turn

332 – 334

3

Helix

335 – 337

3

Helix

356 – 360

5

Turn

365 – 367

3

Helix

368 – 380

13

Beta strand

382 – 389

8

Helix

392 – 394

3

Helix

404 – 406

3

Helix

410 – 423

14

Beta strand

425 – 427

3

Helix

428 – 440

13

Helix

442 – 445

4

Turn

455 – 459

5

Helix

473 – 477

5

Helix

481 – 486

6

Helix

491 – 504

14

Helix

506 – 509

4

Beta strand

513 – 519

7

Beta strand

523 – 532

10

Beta strand

535 – 542

8

Beta strand

544 – 546

3

Beta strand

559 – 566

8

Turn

568 – 570

3

Beta strand

583 – 588

6

Sequences

	Sequence		Length	Mass (Da)
	P53051 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 08869180588053B6	FASTA	589	68,592
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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], MASS SPECTROMETRY. 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], MASS SPECTROMETRY.
[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.

PIR

S59370.

RefSeq

NP_011803.3. NM_001181416.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P53051.

SMR

P53051. Positions 4-589.

ModBase

Search...

Protein-protein interaction databases

IntAct

P53051. 5 interactions.

MINT

MINT-4083809.

STRING

4932.YGR287C.

Protein family/group databases

CAZy

GH13. Glycoside Hydrolase Family 13.

mycoCLAP

OGL13A_YEAST.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR287C; YGR287C; YGR287C.

GeneID

853204.

KEGG

sce:YGR287C.
sce:YGR296W.

Organism-specific databases

CYGD

YGR287c.

SGD

S000003519. IMA1.

Phylogenomic databases

GeneTree

ENSGT00530000063127.

HOGENOM

HOG000220641.

KO

K01187.

OMA

IWITPMY.

OrthoDB

EOG4K0TWQ.

Gene expression databases

ArrayExpress

P53051.

Genevestigator

P53051.

GermOnline

YGR287C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.

InterPro

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]

PANTHER

PTHR10357. PTHR10357. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
[Graphical view]

SMART

SM00642. Aamy. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

BindingDB

P53051.

ChEMBL

CHEMBL5848.

EvolutionaryTrace

P53051.

NextBio

973383.

Entry information

Entry name

MALX3_YEAST

Accession

Primary (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:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program