IMA2_YEAST
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 03-AUG-2022, entry version 148.
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; Q08295; -.
DR PRIDE; Q08295; -.
DR EnsemblFungi; YOL157C_mRNA; YOL157C; YOL157C.
DR GeneID; 854008; -.
DR KEGG; sce:YOL157C; -.
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; PFQWTGG; -.
DR BioCyc; YEAST:G3O-33545-MON; -.
DR BRENDA; 3.2.1.10; 984.
DR Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
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: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 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
