MALX2_YEAST
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 03-AUG-2022, entry version 75.
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;
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 RefSeq; NP_012314.1; NM_001181654.1.
DR AlphaFoldDB; P0CW40; -.
DR SMR; P0CW40; -.
DR BioGRID; 33561; 14.
DR BioGRID; 34824; 5.
DR STRING; 4932.YIL172C; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; P0CW40; -.
DR PRIDE; P0CW40; -.
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 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; DNKEYGA; -.
DR BioCyc; YEAST:YIL172C-MON; -.
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: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 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