ID   MALT_CANAX              Reviewed;         570 AA.
AC   Q02751;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
GN   Name=MAL2; Synonyms=MAL1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-27.
RC   STRAIN=ATCC 32354 / B311;
RX   PubMed=1400249; DOI=10.1128/jb.174.21.6992-6996.1992;
RA   Geber A., Williamson P.R., Rex J.H., Sweeney E.C., Bennett J.E.;
RT   "Cloning and characterization of a Candida albicans maltase gene involved
RT   in sucrose utilization.";
RL   J. Bacteriol. 174:6992-6996(1992).
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   -!- INDUCTION: By maltose and sucrose. Repressed by glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; M94674; AAA34350.2; -; mRNA.
DR   PIR; A45249; A45249.
DR   AlphaFoldDB; Q02751; -.
DR   SMR; Q02751; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CLAE; AGL13B_CANAL; -.
DR   PRIDE; Q02751; -.
DR   VEuPathDB; FungiDB:CAWG_02336; -.
DR   VEuPathDB; FungiDB:CR_10790W_A; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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   Direct protein sequencing; Glycosidase; Hydrolase; Maltose metabolism.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1400249"
FT   CHAIN           2..570
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000054327"
FT   ACT_SITE        206
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            338
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   570 AA;  66210 MW;  F688281082968887 CRC64;
     MSEHKWWKEA VVYQIWPASY KDSNGDGVGD IPGIISTLDY IASLGVTTVW LSPMYDSPQD
     DMGYDVSDYE NVYSKYGTLQ DMDRLIAGCH DRGLKLILDL VINHTSVEHK WFKESRSSKD
     NPKRDWYIWK PPRIDSNGNK HPPNNWGSYF SGSAWKYDEL TGEYYLHLFA ESQPDLNWEN
     KECREAIYNS AIKFWLDKGV DGFRIDTAGM YSKYQHFKDA PVAFPDTEFQ PCEIYHKNGP
     RIHEFHKEMA KVMEPYDTMT VGEVGHSTRE QALKYVSAAE KEMNMMFLFD VVELGSDPRD
     RFRYNGFDLV DLKKAIKSQG EFAEGTDAWS TVFIENHDQA RAISRFGNDS PEFRVLSGKA
     IAMLQCCLTG TLFIYQGQEI GMTNVPRSWP IEEYKDINTI NYYRAFKEKY GKDADYKQKE
     EKLVDVINRL ARDNARTPVQ WSHQQYAGFS EVEPWMRVND NYKEINVEDQ DGDDHSLLNF
     YRKLLKLRGE YKDLFVYGEM KFLDFDDKKL FTFAKEAPGS PVAYIVINFS GEDVKFEPLI
     KGNYKLVLTN VDKDSKDALS PYEARMYVVD