MAL32_YEAST
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 03-AUG-2022, entry version 174.
DE RecName: Full=Alpha-glucosidase MAL32;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
GN Name=MAL32; Synonyms=MAL3S; OrderedLocusNames=YBR299W; 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; P38158; -.
DR PRIDE; P38158; -.
DR TopDownProteomics; P38158; -.
DR EnsemblFungi; YBR299W_mRNA; YBR299W; YBR299W.
DR GeneID; 852602; -.
DR KEGG; sce:YBR299W; -.
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; FYQIHPE; -.
DR BioCyc; YEAST:YBR299W-MON; -.
DR BRENDA; 3.2.1.20; 984.
DR Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
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:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005987; P:sucrose catabolic process; IDA:SGD.
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 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
