ID   MAL32_YEAST             Reviewed;         584 AA.
AC   P38158; D6VQU5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Alpha-glucosidase MAL32;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
GN   Name=MAL32; Synonyms=MAL3S; OrderedLocusNames=YBR299W;
GN   ORFNames=YBR2117;
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=7483839; DOI=10.1002/yea.320110707;
RA   Feuermann M., Charbonnel L., De Montigny J., Bloch J.C., Potier S.,
RA   Souciet J.-L.;
RT   "Sequence of a 9.8 kb segment of yeast chromosome II including the three
RT   genes of the MAL3 locus and three unidentified open reading frames.";
RL   Yeast 11:667-672(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- MISCELLANEOUS: Present with 4030 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; Z36168; CAA85264.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07415.1; -; Genomic_DNA.
DR   PIR; S46183; S46183.
DR   RefSeq; NP_009858.3; NM_001178647.3.
DR   PDB; 1VAD; X-ray; 2.50 A; P=438-446.
DR   PDBsum; 1VAD; -.
DR   AlphaFoldDB; P38158; -.
DR   SMR; P38158; -.
DR   BioGRID; 32992; 58.
DR   DIP; DIP-6822N; -.
DR   IntAct; P38158; 4.
DR   STRING; 4932.YBR299W; -.
DR   BindingDB; P38158; -.
DR   Allergome; 8262; Sac c Glucosidase.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   MaxQB; P38158; -.
DR   PaxDb; 4932-YBR299W; -.
DR   PeptideAtlas; P38158; -.
DR   TopDownProteomics; P38158; -.
DR   EnsemblFungi; YBR299W_mRNA; YBR299W; YBR299W.
DR   GeneID; 852602; -.
DR   KEGG; sce:YBR299W; -.
DR   AGR; SGD:S000000503; -.
DR   SGD; S000000503; MAL32.
DR   VEuPathDB; FungiDB:YBR299W; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   GeneTree; ENSGT00940000176291; -.
DR   HOGENOM; CLU_006462_2_3_1; -.
DR   InParanoid; P38158; -.
DR   OMA; LMYEWRD; -.
DR   OrthoDB; 3680211at2759; -.
DR   BioCyc; YEAST:YBR299W-MONOMER; -.
DR   BRENDA; 3.2.1.20; 984.
DR   BioGRID-ORCS; 852602; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P38158; -.
DR   PRO; PR:P38158; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38158; Protein.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0033934; F:glucan 1,4-alpha-maltotriohydrolase activity; IDA:SGD.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IDA:SGD.
DR   GO; GO:0004574; F:oligo-1,6-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:SGD.
DR   GO; GO:0000025; P:maltose catabolic process; IDA:SGD.
DR   GO; GO:0005987; P:sucrose catabolic process; IDA:SGD.
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   1: Evidence at protein level;
KW   3D-structure; Glycosidase; Hydrolase; Maltose metabolism;
KW   Reference proteome.
FT   CHAIN           1..584
FT                   /note="Alpha-glucosidase MAL32"
FT                   /id="PRO_0000054329"
FT   ACT_SITE        214
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        276
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            349
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   584 AA;  68142 MW;  4C461F5F40B464C3 CRC64;
     MTISDHPETE PKWWKEATIY QIYPASFKDS NNDGWGDLKG ITSKLQYIKD LGVDAIWVCP
     FYDSPQQDMG YDISNYEKVW PTYGTNEDCF ELIDKTHKLG MKFITDLVIN HCSTEHEWFK
     ESRSSKTNPK RDWFFWRPPK GYDAEGKPIP PNNWKSFFGG SAWTFDETTN EFYLRLFASR
     QVDLNWENED CRRAIFESAV GFWLDHGVDG FRIDTAGLYS KRPGLPDSPI FDKTSKLQHP
     NWGSHNGPRI HEYHQELHRF MKNRVKDGRE IMTVGEVAHG SDNALYTSAA RYEVSEVFSF
     THVELGTSPF FRYNIVPFTL KQWKEAIASN FLFINGTDSW ATTYIENHDQ ARSITRFADD
     SPKYRKISGK LLTLLECSLT GTLYVYQGQE IGQINFKEWP IEKYEDVDVK NNYEIIKKSF
     GKNSKEMKDF FKGIALLSRD HSRTPMPWTK DKPNAGFTGP DVKPWFFLNE SFEQGINVEQ
     ESRDDDSVLN FWKRALQARK KYKELMIYGY DFQFIDLDSD QIFSFTKEYE DKTLFAALNF
     SGEEIEFSLP REGASLSFIL GNYDDTDVSS RVLKPWEGRI YLVK
//