ID MALX3_YEAST Reviewed; 589 AA. AC P53051; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 65. DE RecName: Full=Probable alpha-glucosidase FSP2; DE EC=3.2.1.20; DE AltName: Full=Maltase; DE AltName: Full=Flocculent-specific protein 2; GN Name=FSP2; OrderedLocusNames=YGR287C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tonouchi A.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97245295; PubMed=9090054; RX DOI=10.1002/(SICI)1097-0061(19970315)13:3<251::AID-YEA63>3.3.CO;2-I; RA Volckaert G., Voet M., Robben J.; RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the RT right arm of chromosome VII from Saccharomyces cerevisiae carrying the RT MAL1 locus reveals 15 complete open reading frames, including ZUO1, RT BGL2 and BIO2 genes and an ABC transporter gene."; RL Yeast 13:251-259(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313265; PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., RA Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., RA Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., RA Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., RA Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., RA Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., RA Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., RA Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., RA Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., RA Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., RA Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., RA Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., RA Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., RA Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., RA Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., RA Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., RA Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., RA Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., RA Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., RA van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., RA Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., RA Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., RA Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Probable alpha-glucosidase involved in maltose CC metabolism. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing (1->4)- CC linked alpha-D-glucose residues with release of alpha-D-glucose. CC -!- INTERACTION: CC P22696:ESS1; NbExp=1; IntAct=EBI-10464, EBI-6679; CC P33203:PRP40; NbExp=1; IntAct=EBI-10464, EBI-701; CC P39940:RSP5; NbExp=1; IntAct=EBI-10464, EBI-16219; CC P40318:SSM4; NbExp=1; IntAct=EBI-10464, EBI-18208; CC Q06525:URN1; NbExp=1; IntAct=EBI-10464, EBI-35138; CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D43761; BAA07818.1; -; Genomic_DNA. DR EMBL; Z73072; CAA97319.1; -; Genomic_DNA. DR EMBL; Z73073; CAA97321.1; -; Genomic_DNA. DR PIR; S59370; S59370. DR RefSeq; NP_011803.1; -. DR HSSP; P21332; 1UOK. DR IntAct; P53051; 5. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR Ensembl; YGR287C; Saccharomyces cerevisiae. DR GeneID; 853204; -. DR GenomeReviews; Y13135_GR; YGR287C. DR KEGG; sce:YGR287C; -. DR NMPDR; fig|4932.3.peg.2934; -. DR CYGD; YGR287c; -. DR SGD; S000003519; YGR287C. DR HOGENOM; P53051; -. DR OMA; P53051; WENEVTR. DR BRENDA; 3.2.1.20; 250. DR NextBio; 973383; -. DR ArrayExpress; P53051; -. DR GermOnline; YGR287C; Saccharomyces cerevisiae. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0004558; F:alpha-glucosidase activity; IEA:EC. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0004574; F:oligo-1,6-glucosidase activity; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0000023; P:maltose metabolic process; IC:SGD. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat. DR InterPro; IPR006589; Glyco_hydro_13_sub_cat. DR InterPro; IPR013781; Glyco_hydro_sg_catalytic. DR Gene3D; G3DSA:2.60.40.1180; Glyco_hydro_13_b; 1. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycosidase; Hydrolase; Maltose metabolism. FT CHAIN 1 589 Probable alpha-glucosidase FSP2. FT /FTId=PRO_0000054333. FT ACT_SITE 215 215 Nucleophile (By similarity). FT ACT_SITE 277 277 Proton donor (By similarity). FT ACT_SITE 352 352 By similarity. SQ SEQUENCE 589 AA; 68592 MW; 08869180588053B6 CRC64; MTISSAHPET EPKWWKEATF YQIYPASFKD SNDDGWGDMK GIASKLEYIK ELGADAIWIS PFYDSPQDDM GYDIANYEKV WPTYGTNEDC FALIEKTHKL GMKFITDLVI NHCSSEHEWF KESRSSKTNP KRDWFFWRPP KGYDAEGKPI PPNNWKSYFG GSAWTFDEKT QEFYLRLFCS TQPDLNWENE DCRKAIYESA VGYWLDHGVD GFRIDVGSLY SKVVGLPDAP VVDKNSTWQS SDPYTLNGPR IHEFHQEMNQ FIRNRVKDGR EIMTVGEMQH ASDETKRLYT SASRHELSEL FNFSHTDVGT SPLFRYNLVP FELKDWKIAL AELFRYINGT DCWSTIYLEN HDQPRSITRF GDDSPKNRVI SGKLLSVLLS ALTGTLYVYQ GQELGQINFK NWPVEKYEDV EIRNNYNAIK EEHGENSEEM KKFLEAIALI SRDHARTPMQ WSREEPNAGF SGPSAKPWFY LNDSFREGIN VEDEIKDPNS VLNFWKEALK FRKAHKDITV YGYDFEFIDL DNKKLFSFTK KYNNKTLFAA LNFSSDATDF KIPNDDSSFK LEFGNYPKKE VDASSRTLKP WEGRIYISE //