ID   MAL12_YEAST             Reviewed;         584 AA.
AC   P53341; D6VV67;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Alpha-glucosidase MAL12;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
GN   Name=MAL12; Synonyms=MAL1S; OrderedLocusNames=YGR292W;
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 96604 / S288c / FY1679;
RX   PubMed=9090054;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA   Volckaert G., Voet M., Robben J.;
RT   "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT   arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT   reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT   genes and an ABC transporter gene.";
RL   Yeast 13:251-259(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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 5060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; Z73077; CAA97325.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08378.1; -; Genomic_DNA.
DR   PIR; S64627; S64627.
DR   RefSeq; NP_011808.3; NM_001181421.3.
DR   AlphaFoldDB; P53341; -.
DR   SMR; P53341; -.
DR   BioGRID; 33540; 253.
DR   DIP; DIP-4890N; -.
DR   IntAct; P53341; 2.
DR   STRING; 4932.YGR292W; -.
DR   BindingDB; P53341; -.
DR   ChEMBL; CHEMBL2932; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CLAE; AGL13L_YEAST; -.
DR   MaxQB; P53341; -.
DR   PaxDb; 4932-YGR292W; -.
DR   PeptideAtlas; P53341; -.
DR   TopDownProteomics; P53341; -.
DR   EnsemblFungi; YGR292W_mRNA; YGR292W; YGR292W.
DR   GeneID; 853209; -.
DR   KEGG; sce:YGR292W; -.
DR   AGR; SGD:S000003524; -.
DR   SGD; S000003524; MAL12.
DR   VEuPathDB; FungiDB:YGR292W; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   GeneTree; ENSGT00940000176291; -.
DR   HOGENOM; CLU_006462_2_3_1; -.
DR   InParanoid; P53341; -.
DR   OMA; FHYADID; -.
DR   OrthoDB; 3680211at2759; -.
DR   BioCyc; YEAST:YGR292W-MONOMER; -.
DR   BRENDA; 2.4.1.B65; 984.
DR   BRENDA; 3.2.1.20; 984.
DR   BioGRID-ORCS; 853209; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53341; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53341; 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; IGI:SGD.
DR   GO; GO:0005987; P:sucrose catabolic process; IGI: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   Glycosidase; Hydrolase; Maltose metabolism; Reference proteome.
FT   CHAIN           1..584
FT                   /note="Alpha-glucosidase MAL12"
FT                   /id="PRO_0000054328"
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;  68094 MW;  B10FCD5A5E423211 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
     THVEVGTSPF FRYNIVPFTL KQWKEAIASN FLFINGTDSW ATTYIENHDQ ARSITRFADD
     SPKYRKISGK LLTLLECSLT GTLYVYQGQE IGQINFKEWP IEKYEDVDVK NNYEIIKKSF
     GKNSKEMKDF FKGIALLSRD HSRTPMPWTK DKPNAGFTGP DVKPWFLLNE SFEQGINVEQ
     ESRDDDSVLN FWKRALQARK KYKELMIYGY DFQFIDLDSD QIFSFTKEYE DKTLFAALNF
     SGEEIEFSLP REGASLSFIL GNYDDTDVSS RVLKPWEGRI YLVK
//