ID   IMA2_YEAST              Reviewed;         589 AA.
AC   Q08295; D6W1R3;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Oligo-1,6-glucosidase IMA2;
DE            EC=3.2.1.10;
DE   AltName: Full=Alpha-glucosidase;
DE   AltName: Full=Isomaltase 2;
GN   Name=IMA2; OrderedLocusNames=YOL157C;
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=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   INDUCTION.
RX   PubMed=11389906; DOI=10.1016/s0014-5793(01)02503-0;
RA   Alexandre H., Ansanay-Galeote V., Dequin S., Blondin B.;
RT   "Global gene expression during short-term ethanol stress in Saccharomyces
RT   cerevisiae.";
RL   FEBS Lett. 498:98-103(2001).
RN   [4]
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 specificity for isomaltase, methyl-
CC       alpha-glucoside, and palatinose. {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   -!- INDUCTION: By ethanol. {ECO:0000269|PubMed:11389906}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; Z74899; CAA99179.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10629.1; -; Genomic_DNA.
DR   PIR; S66856; S66856.
DR   RefSeq; NP_014485.1; NM_001183410.1.
DR   AlphaFoldDB; Q08295; -.
DR   SMR; Q08295; -.
DR   BioGRID; 34261; 54.
DR   IntAct; Q08295; 1.
DR   STRING; 4932.YOL157C; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CLAE; OGL13B_YEAST; -.
DR   PaxDb; 4932-YOL157C; -.
DR   PeptideAtlas; Q08295; -.
DR   EnsemblFungi; YOL157C_mRNA; YOL157C; YOL157C.
DR   GeneID; 854008; -.
DR   KEGG; sce:YOL157C; -.
DR   AGR; SGD:S000005517; -.
DR   SGD; S000005517; IMA2.
DR   VEuPathDB; FungiDB:YOL157C; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   GeneTree; ENSGT00940000176291; -.
DR   HOGENOM; CLU_006462_1_1_1; -.
DR   InParanoid; Q08295; -.
DR   OMA; FYQIHPE; -.
DR   OrthoDB; 3680211at2759; -.
DR   BioCyc; YEAST:G3O-33545-MONOMER; -.
DR   BRENDA; 3.2.1.10; 984.
DR   Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
DR   BioGRID-ORCS; 854008; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q08295; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q08295; Protein.
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; 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   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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   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   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Maltose metabolism; Reference proteome.
FT   CHAIN           1..589
FT                   /note="Oligo-1,6-glucosidase IMA2"
FT                   /id="PRO_0000245259"
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;  68625 MW;  E2E2D77A2A77C75A CRC64;
     MTISSAHPET EPKWWKEATI YQIYPASFKD SNNDGWGDMK GIASKLEYIK ELGADAIWIS
     PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL GMKFITDLVI NHCSSEHEWF
     KESRSSKTNP KRDWFFWRPP KGYDAEGKPI PPNNWRSYFG GSAWTFDEKT QEFYLRLFCS
     TQPDLNWENE DCRKAIYESA VGYWLDHGVD GFRIDVGSLY SKVAGLPDAP VIDENSKWQP
     SDPFTMNGPR IHEFHQEMNK FIRNRVKDGR EIMTVGEMQH 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
//