MAL12_YEAST
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 03-AUG-2022, entry version 167.
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}.
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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; 252.
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; P53341; -.
DR TopDownProteomics; P53341; -.
DR EnsemblFungi; YGR292W_mRNA; YGR292W; YGR292W.
DR GeneID; 853209; -.
DR KEGG; sce:YGR292W; -.
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; MNNHDVP; -.
DR BioCyc; YEAST:YGR292W-MON; -.
DR BRENDA; 2.4.1.B65; 984.
DR BRENDA; 3.2.1.20; 984.
DR Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
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:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005987; P:sucrose catabolic process; IGI: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 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
