ID MALX4_YEAST Reviewed; 589 AA. AC P0CW41; D6VVX6; P40439; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 1. DT 13-SEP-2023, entry version 74. DE RecName: Full=Oligo-1,6-glucosidase IMA4; DE EC=3.2.1.10; DE AltName: Full=Alpha-glucosidase; DE AltName: Full=Flocculent-specific protein 2; DE AltName: Full=Isomaltase 4; GN Name=IMA4; Synonyms=FSP2; OrderedLocusNames=YJL221C; GN ORFNames=HRE589, J0218; 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 [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7725802; DOI=10.1002/yea.320101216; RA Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.; RT "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere RT of yeast chromosome X."; RL Yeast 10:1657-1662(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."; RL EMBO J. 15:2031-2049(1996). RN [3] 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 [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 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z34098; CAA83990.1; -; Genomic_DNA. DR EMBL; Z49496; CAA89517.1; -; Genomic_DNA. DR EMBL; BK006943; DAA08592.1; -; Genomic_DNA. DR PIR; S50355; S50355. DR RefSeq; NP_012096.1; NM_001179518.1. DR RefSeq; NP_012314.1; NM_001181654.1. DR AlphaFoldDB; P0CW41; -. DR SMR; P0CW41; -. DR BioGRID; 33561; 14. DR BioGRID; 34824; 5. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblFungi; YIL172C_mRNA; YIL172C; YIL172C. DR EnsemblFungi; YJL221C_mRNA; YJL221C; YJL221C. DR GeneID; 853235; -. DR GeneID; 854635; -. DR KEGG; sce:YIL172C; -. DR KEGG; sce:YJL221C; -. DR AGR; SGD:S000003757; -. DR SGD; S000003757; IMA4. DR VEuPathDB; FungiDB:YIL172C; -. DR VEuPathDB; FungiDB:YJL221C; -. DR GeneTree; ENSGT00940000176291; -. DR HOGENOM; CLU_006462_1_1_1; -. DR InParanoid; P0CW41; -. DR OrthoDB; 3680211at2759; -. DR BioCyc; YEAST:YJL221C-MONOMER; -. DR Reactome; R-SCE-352230; Amino acid transport across the plasma membrane. DR PRO; PR:P0CW41; -. DR Proteomes; UP000002311; Chromosome X. DR RNAct; P0CW41; 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; IMP:SGD. DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central. 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 3: Inferred from homology; KW Glycosidase; Hydrolase; Maltose metabolism; Reference proteome. FT CHAIN 1..589 FT /note="Oligo-1,6-glucosidase IMA4" FT /id="PRO_0000408197" 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 //