ID   MAL62_YEASX             Reviewed;         584 AA.
AC   P07265;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Alpha-glucosidase MAL62;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
GN   Name=MAL62; Synonyms=MAL6S;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Carlsbergensis / CB11;
RX   PubMed=3516795; DOI=10.1016/0378-1119(86)90269-6;
RA   Hong S.H., Marmur J.;
RT   "Primary structure of the maltase gene of the MAL6 locus of Saccharomyces
RT   carlsbergensis.";
RL   Gene 41:75-84(1986).
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   -!- 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; M12601; AAA34757.1; -; Genomic_DNA.
DR   PIR; S05847; ALBY.
DR   PDB; 1G7P; X-ray; 1.50 A; P=438-446.
DR   PDBsum; 1G7P; -.
DR   AlphaFoldDB; P07265; -.
DR   SMR; P07265; -.
DR   BindingDB; P07265; -.
DR   ChEMBL; CHEMBL4357; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   SGD; S000029690; MAL62.
DR   VEuPathDB; FungiDB:YGR292W; -.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046352; P:disaccharide catabolic process; IEA:UniProt.
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.
FT   CHAIN           1..584
FT                   /note="Alpha-glucosidase MAL62"
FT                   /id="PRO_0000054330"
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;  68183 MW;  D091CCCC63E58765 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 IMRVGEVAHG SDNALYTSAA RYEVSEVFSF
     THVEVGTSPF 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