ID   MALX2_YEAST             Reviewed;         589 AA.
AC   P0CW40; D6VVX6; P40439;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   04-NOV-2026, entry version 91.
DE   RecName: Full=Oligo-1,6-glucosidase IMA3;
DE            EC=3.2.1.10;
DE   AltName: Full=Alpha-glucosidase;
DE   AltName: Full=Isomaltase 3;
GN   Name=IMA3; OrderedLocusNames=YIL172C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870; DOI=10.1038/387s084;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [2]
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   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [4]
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   [5]
RP   FUNCTION.
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).
CC   -!- FUNCTION: Alpha-glucosidase with broad substrate specificity for alpha-
CC       1,4- and alpha-1,6-glucosides. Not required for isomaltose utilization,
CC       but overexpression allows the IMA1 null mutant to grow on isomaltose.
CC       {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 166 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; Z46921; CAA87020.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08385.1; -; Genomic_DNA.
DR   PIR; S50355; S50355.
DR   RefSeq; NP_012096.1; NM_001179518.1.
DR   AlphaFoldDB; P0CW40; -.
DR   SMR; P0CW40; -.
DR   BioGRID; 33561; 14.
DR   BioGRID; 34824; 6.
DR   FunCoup; P0CW40; 1133.
DR   STRING; 4932.YIL172C; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 4932-YIL172C; -.
DR   PeptideAtlas; P0CW40; -.
DR   EnsemblFungi; YIL172C_mRNA; YIL172C; YIL172C.
DR   EnsemblFungi; YJL221C_mRNA; YJL221C; YJL221C.
DR   GeneID; 854635; -.
DR   KEGG; sce:YIL172C; -.
DR   KEGG; sce:YJL221C; -.
DR   AGR; SGD:S000001434; -.
DR   SGD; S000001434; IMA3.
DR   VEuPathDB; FungiDB:YIL172C; -.
DR   VEuPathDB; FungiDB:YJL221C; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_1_1_1; -.
DR   InParanoid; P0CW40; -.
DR   OMA; ADDSAWW; -.
DR   OrthoDB; 1740265at2759; -.
DR   BioCyc; YEAST:YIL172C-MONOMER; -.
DR   BRENDA; 3.2.1.10; 984.
DR   Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
DR   PRO; PR:P0CW40; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P0CW40; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004558; F:alpha-1,4-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; IGI:SGD.
DR   GO; GO:0000025; P:maltose catabolic process; IBA:GO_Central.
DR   GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   FunFam; 3.20.20.80:FF:000064; Oligo-1,6-glucosidase; 1.
DR   FunFam; 3.90.400.10:FF:000004; Oligo-1,6-glucosidase; 1.
DR   FunFam; 2.60.40.1180:FF:000027; Oligo-1,6-glucosidase IMA1; 1.
DR   FunFam; 3.20.20.80:FF:000087; Oligo-1,6-glucosidase IMA1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 3.90.400.10; Oligo-1,6-glucosidase, Domain 2; 1.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosidase; Hydrolase; Maltose metabolism; Reference proteome.
FT   CHAIN           1..589
FT                   /note="Oligo-1,6-glucosidase IMA3"
FT                   /id="PRO_0000054332"
FT   ACT_SITE        215
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            352
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   589 AA;  68699 MW;  0323A2677148EC29 CRC64;
     MTISSAHPET EPKWWKEATI YQIYPASFKD SNNDGWGDMK GIASKLEYIK ELGTDAIWIS
     PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL GMKFITDLVI NHCSSEHEWF
     KESRSSKTNP KRDWFFWRPP KGYDAEGKPI PPNNWRSYFG GSAWTFDEKT QEFYLRLFCS
     TQPDLNWENE DCRKAIYESA VGYWLDHGVD GFRIDVGSLY SKVAGLPDAP VIDENSKWQL
     SDPFTMNGPR IHEFHQEMNK FIRNRVKDGR EIMTVGEMRH ATDETKRLYT SASRHELSEL
     FNFSHTDVGT SPKFRQNLIP YELKDWKVAL AELFRYVNGT DCWSTIYLEN HDQPRSITRF
     GDDSPKNRVI SGKLLSVLLV SLSGTLYVYQ GQELGEINFK NWPIEKYEDV EVRNNYDAIK
     EEHGENSKEM KRFLEAIALI SRDHARTPMQ WSREEPNAGF SGPNAKPWFY LNESFREGIN
     AEDESKDPNS VLNFWKEALR FRKAHKDITV YGYDFEFIDL DNKKLFSFTK KYDNKTLFAA
     LNFSSDSIDF TIPNNSSSFK LEFGNYPRSE VDASSRTLKP WEGRIYISE
//