MALX3_YEAST
ID MALX3_YEAST Reviewed; 589 AA.
AC P53051; D6VV64; Q76CZ0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Oligo-1,6-glucosidase IMA1;
DE EC=3.2.1.10;
DE AltName: Full=Alpha-glucosidase;
DE AltName: Full=Isomaltase 1;
GN Name=IMA1; OrderedLocusNames=YGR287C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-13; 161-169; 247-258;
RP 288-294; 314-320 AND 577-584, FUNCTION, AND MUTAGENESIS OF ASP-215;
RP VAL-216; GLY-217 AND SER-218.
RC STRAIN=ATCC 56960 / D-346;
RX PubMed=15291818; DOI=10.1111/j.1432-1033.2004.04276.x;
RA Yamamoto K., Nakayama A., Yamamoto Y., Tabata S.;
RT "Val216 decides the substrate specificity of alpha-glucosidase in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 271:3414-3420(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tonouchi A.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=20562106; DOI=10.1074/jbc.m110.145946;
RA Teste M.A., Francois J.M., Parrou J.L.;
RT "Characterization of a new multigene family encoding isomaltases in the
RT yeast Saccharomyces cerevisiae, the IMA family.";
RL J. Biol. Chem. 285:26815-26824(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MALTOSE.
RX PubMed=20812985; DOI=10.1111/j.1742-4658.2010.07810.x;
RA Yamamoto K., Miyake H., Kusunoki M., Osaki S.;
RT "Crystal structures of isomaltase from Saccharomyces cerevisiae and in
RT complex with its competitive inhibitor maltose.";
RL FEBS J. 277:4205-4214(2010).
CC -!- FUNCTION: Major isomaltase (alpha-1,6-glucosidase) required for
CC isomaltose utilization. Preferentially hydrolyzes isomaltose,
CC palatinose, and methyl-alpha-glucoside, with little activity towards
CC isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.
CC {ECO:0000269|PubMed:15291818, ECO:0000269|PubMed:20562106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
CC oligosaccharides produced from starch and glycogen by alpha-amylase,
CC and in isomaltose.; EC=3.2.1.10;
CC -!- INTERACTION:
CC P53051; P39940: RSP5; NbExp=2; IntAct=EBI-10464, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14576278}.
CC -!- INDUCTION: Expression is increased in response to the addition of
CC maltose, isomaltose, and alpha-methylglucopyranoside.
CC {ECO:0000269|PubMed:20562106}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AB109221; BAD00094.1; -; mRNA.
DR EMBL; D43761; BAA07818.1; -; Genomic_DNA.
DR EMBL; Z73072; CAA97319.1; -; Genomic_DNA.
DR EMBL; Z73073; CAA97321.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08375.1; -; Genomic_DNA.
DR PIR; S59370; S59370.
DR RefSeq; NP_011803.3; NM_001181416.3.
DR PDB; 3A47; X-ray; 1.59 A; A=1-589.
DR PDB; 3A4A; X-ray; 1.60 A; A=1-589.
DR PDB; 3AJ7; X-ray; 1.30 A; A=1-589.
DR PDB; 3AXH; X-ray; 1.80 A; A=1-589.
DR PDB; 3AXI; X-ray; 1.40 A; A=1-589.
DR PDBsum; 3A47; -.
DR PDBsum; 3A4A; -.
DR PDBsum; 3AJ7; -.
DR PDBsum; 3AXH; -.
DR PDBsum; 3AXI; -.
DR AlphaFoldDB; P53051; -.
DR SMR; P53051; -.
DR BioGRID; 33537; 60.
DR IntAct; P53051; 5.
DR STRING; 4932.YGR287C; -.
DR BindingDB; P53051; -.
DR ChEMBL; CHEMBL5848; -.
DR DrugCentral; P53051; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CLAE; OGL13C_YEAST; -.
DR iPTMnet; P53051; -.
DR MaxQB; P53051; -.
DR PaxDb; P53051; -.
DR PRIDE; P53051; -.
DR EnsemblFungi; YGR287C_mRNA; YGR287C; YGR287C.
DR GeneID; 853204; -.
DR KEGG; sce:YGR287C; -.
DR SGD; S000003519; IMA1.
DR VEuPathDB; FungiDB:YGR287C; -.
DR eggNOG; KOG0471; Eukaryota.
DR GeneTree; ENSGT00940000176291; -.
DR HOGENOM; CLU_006462_1_1_1; -.
DR InParanoid; P53051; -.
DR OMA; PNGEKWA; -.
DR BioCyc; YEAST:YGR287C-MON; -.
DR BRENDA; 3.2.1.10; 984.
DR Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
DR EvolutionaryTrace; P53051; -.
DR PRO; PR:P53051; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53051; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0033934; F:glucan 1,4-alpha-maltotriohydrolase activity; IBA:GO_Central.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004574; F:oligo-1,6-glucosidase activity; IDA:SGD.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:SGD.
DR GO; GO:0046352; P:disaccharide catabolic process; IMP:SGD.
DR GO; GO:0000025; P:maltose catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Maltose metabolism; Mitochondrion; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15291818"
FT CHAIN 2..589
FT /note="Oligo-1,6-glucosidase IMA1"
FT /id="PRO_0000054333"
FT ACT_SITE 215
FT /note="Nucleophile"
FT ACT_SITE 277
FT /note="Proton donor"
FT SITE 352
FT /note="Transition state stabilizer"
FT MUTAGEN 215
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:15291818"
FT MUTAGEN 216
FT /note="V->T: Can also hydrolyze maltose."
FT /evidence="ECO:0000269|PubMed:15291818"
FT MUTAGEN 217
FT /note="G->A: Does not alter substrate specificity."
FT /evidence="ECO:0000269|PubMed:15291818"
FT MUTAGEN 218
FT /note="S->G: Does not alter substrate specificity."
FT /evidence="ECO:0000269|PubMed:15291818"
FT CONFLICT 428
FT /note="E -> D (in Ref. 1; BAD00094)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 323..331
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 428..440
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 455..459
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 473..477
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 481..486
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 491..504
FT /evidence="ECO:0007829|PDB:3AJ7"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 523..532
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 559..566
FT /evidence="ECO:0007829|PDB:3AJ7"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:3AJ7"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:3AJ7"
SQ SEQUENCE 589 AA; 68592 MW; 08869180588053B6 CRC64;
MTISSAHPET EPKWWKEATF YQIYPASFKD SNDDGWGDMK GIASKLEYIK ELGADAIWIS
PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL GMKFITDLVI NHCSSEHEWF
KESRSSKTNP KRDWFFWRPP KGYDAEGKPI PPNNWKSYFG GSAWTFDEKT QEFYLRLFCS
TQPDLNWENE DCRKAIYESA VGYWLDHGVD GFRIDVGSLY SKVVGLPDAP VVDKNSTWQS
SDPYTLNGPR IHEFHQEMNQ FIRNRVKDGR EIMTVGEMQH ASDETKRLYT SASRHELSEL
FNFSHTDVGT SPLFRYNLVP FELKDWKIAL AELFRYINGT DCWSTIYLEN HDQPRSITRF
GDDSPKNRVI SGKLLSVLLS ALTGTLYVYQ GQELGQINFK NWPVEKYEDV EIRNNYNAIK
EEHGENSEEM KKFLEAIALI SRDHARTPMQ WSREEPNAGF SGPSAKPWFY LNDSFREGIN
VEDEIKDPNS VLNFWKEALK FRKAHKDITV YGYDFEFIDL DNKKLFSFTK KYNNKTLFAA
LNFSSDATDF KIPNDDSSFK LEFGNYPKKE VDASSRTLKP WEGRIYISE
