MALT_SCHPO
ID MALT_SCHPO Reviewed; 579 AA.
AC Q9P6J3; Q4U125;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Alpha-glucosidase;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
GN Name=mal1; ORFNames=SPBC1683.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REPRESSION BY GLUCOSE AND INOSITOL.
RX PubMed=16967902;
RA Yao S., Chi Z., He S.;
RT "Regulation of MAL1+ gene expression encoding maltase in
RT Schizosaccharomyces pombe by added inositol.";
RL Indian J. Biochem. Biophys. 43:143-147(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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: Repressed by glucose and inositol.
CC {ECO:0000269|PubMed:16967902}.
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; DQ019991; AAY57566.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB91169.1; -; Genomic_DNA.
DR RefSeq; NP_595063.1; NM_001020969.2.
DR AlphaFoldDB; Q9P6J3; -.
DR SMR; Q9P6J3; -.
DR BioGRID; 276520; 8.
DR STRING; 4896.SPBC1683.07.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR MaxQB; Q9P6J3; -.
DR PaxDb; Q9P6J3; -.
DR EnsemblFungi; SPBC1683.07.1; SPBC1683.07.1:pep; SPBC1683.07.
DR GeneID; 2539976; -.
DR KEGG; spo:SPBC1683.07; -.
DR PomBase; SPBC1683.07; mal1.
DR VEuPathDB; FungiDB:SPBC1683.07; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_1_1_1; -.
DR InParanoid; Q9P6J3; -.
DR OMA; VLMVETY; -.
DR PhylomeDB; Q9P6J3; -.
DR PRO; PR:Q9P6J3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0044653; F:dextrin alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0033934; F:glucan 1,4-alpha-maltotriohydrolase activity; IBA:GO_Central.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0004574; F:oligo-1,6-glucosidase activity; IBA:GO_Central.
DR GO; GO:0044654; F:starch alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0044247; P:cellular polysaccharide catabolic process; IC:PomBase.
DR GO; GO:0000025; P:maltose catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Glycosidase; Hydrolase; Maltose metabolism; Reference proteome.
FT CHAIN 1..579
FT /note="Alpha-glucosidase"
FT /id="PRO_0000310319"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 346
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 381
FT /note="F -> L (in Ref. 1; AAY57566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 67752 MW; 7B79064326E445AA CRC64;
MKVVPSEKIK PNWWRETSVY QIYPASFKDS NGDGFGDLEG IISKVDYLKA LNVESIWLCP
IYPSPLKDMG YDVSDYKQID SRYGTLEDLD RLMKALHERD MKLVMDLVLN HTSDQHEWFK
ESRSSKTNPK RDWYFWKPAR YNEKGERLPP NNWRSYFDTS AWEWDEATQE YYLHLWSVGQ
PDLNWETPKV REAVHDILRF WLDRGVDGFR LDAINMISKD QRFLDAPITD DRYEYQLAYQ
YYANGPRIHE YLNGIGNILT EYDAFSVGEM PYVLDTNEIL HVVGADRREL TMIFQFDFVD
LDLDPNQHKY IEGSWELSDL KKSLKKWQSA LLSGGGWNAS FIENHDQTRT VSRYLSDSPK
YRAYSSKLMA LFIIFQSGTP FVFQGQELAL ANIPRDWPID EYLDVETQNF WKLFMSGNPS
QEEIEKTMDI VNKRARDNGR TPMHWDSSPN GGFTKAGVKP WMRVTNDYKE WNAANQVNDP
ESPYTFWSKA LELRKELKDA VVYGSFELIS EEDPSIVAFV RESSTYKLII LLNFTGNKVS
YDCPLNLTSY EILLDNYKDF ICMTSPVTLN PYQAVLLKL
