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Alpha-glucosidase (EC 3.2.1.20) (Maltase)

 AGLU_SCHPO              Reviewed;         969 AA.
Q9C0Y4;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
29-AUG-2001, sequence version 2.
28-FEB-2018, entry version 122.
RecName: Full=Alpha-glucosidase;
EC=3.2.1.20;
AltName: Full=Maltase;
Flags: Precursor;
Name=agl1; Synonyms=agl; ORFNames=SPAPB24D3.10c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36; 175-194;
375-395 AND 427-451, AND MUTAGENESIS OF ASP-218; ASP-287; ASP-355;
ASP-481; GLU-484; ASP-647; ASP-676; GLU-714 AND ASP-877.
PubMed=11298744; DOI=10.1046/j.1432-1327.2001.02104.x;
Okuyama M., Okuno A., Shimizu N., Mori H., Kimura A., Chiba S.;
"Carboxyl group of residue Asp647 as possible proton donor in
catalytic reaction of alpha-glucosidase from Schizosaccharomyces
pombe.";
Eur. J. Biochem. 268:2270-2280(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
-!- FUNCTION: Hydrolyzes malto-oligosaccharides, but has a low
activity toward soluble starch.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing (1->4)-
linked alpha-D-glucose residues with release of alpha-D-glucose.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
{ECO:0000305}.
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EMBL; CU329670; CAC36906.1; -; Genomic_DNA.
EMBL; AB045751; BAB43946.1; -; mRNA.
RefSeq; NP_593996.1; NM_001019422.2.
ProteinModelPortal; Q9C0Y4; -.
STRING; 4896.SPAPB24D3.10c.1; -.
ChEMBL; CHEMBL3784909; -.
CAZy; GH31; Glycoside Hydrolase Family 31.
MaxQB; Q9C0Y4; -.
PaxDb; Q9C0Y4; -.
PRIDE; Q9C0Y4; -.
GeneID; 2543499; -.
KEGG; spo:SPAPB24D3.10c; -.
PomBase; SPAPB24D3.10c; agl1.
HOGENOM; HOG000041175; -.
InParanoid; Q9C0Y4; -.
KO; K01187; -.
OrthoDB; EOG092C0F23; -.
PhylomeDB; Q9C0Y4; -.
BRENDA; 3.2.1.20; 5613.
Reactome; R-SPO-189085; Digestion of dietary carbohydrate.
Reactome; R-SPO-6798695; Neutrophil degranulation.
PRO; PR:Q9C0Y4; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005576; C:extracellular region; IDA:PomBase.
GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0032450; F:maltose alpha-glucosidase activity; IDA:PomBase.
GO; GO:0044654; F:starch alpha-glucosidase activity; IDA:PomBase.
GO; GO:0000025; P:maltose catabolic process; IDA:PomBase.
Gene3D; 2.60.40.1180; -; 2.
InterPro; IPR031727; Gal_mutarotase_N.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR000322; Glyco_hydro_31.
InterPro; IPR030458; Glyco_hydro_31_AS.
InterPro; IPR030459; Glyco_hydro_31_CS.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF01055; Glyco_hydro_31; 1.
Pfam; PF16863; NtCtMGAM_N; 1.
SUPFAM; SSF51445; SSF51445; 2.
SUPFAM; SSF74650; SSF74650; 1.
PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein;
Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:11298744}.
CHAIN 25 969 Alpha-glucosidase.
/FTId=PRO_0000018581.
ACT_SITE 481 481 Nucleophile.
ACT_SITE 484 484
ACT_SITE 647 647 Proton donor.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 462 462 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 470 470 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 523 523 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 589 589 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 648 648 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 801 801 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 810 810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 821 821 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 885 885 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 915 915 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 934 934 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 942 942 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 954 954 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 966 966 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 218 218 D->N: Almost total loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 287 287 D->N: No loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 355 355 D->E,N: Almost total loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 481 481 D->A,E,N: Loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 484 484 E->A,Q: Loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 484 484 E->D: No loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 647 647 D->A,E,N: Loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 676 676 D->N: No loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 714 714 E->Q: No loss of activity.
{ECO:0000269|PubMed:11298744}.
MUTAGEN 877 877 D->N: Almost total loss of activity.
{ECO:0000269|PubMed:11298744}.
CONFLICT 30 30 L -> F (in Ref. 2; CAC36906).
{ECO:0000305}.
CONFLICT 220 220 P -> A (in Ref. 1; BAB43946).
{ECO:0000305}.
CONFLICT 507 507 T -> V (in Ref. 1; BAB43946).
{ECO:0000305}.
CONFLICT 566 566 D -> N (in Ref. 1; BAB43946).
{ECO:0000305}.
SEQUENCE 969 AA; 108686 MW; F3122E2CFA551C25 CRC64;
MMISTAYQSL FLTALFSAIS IAVGNVYQTL NVIGDRNVTI PTNGIPQRLS VYDPYRGVNC
QGYQAVNISE SQNGVTAYLA LLGEPCYAYG TDYPLLFLNV TYEEADRVHI SIKDANNTQF
QFTSRKDLWD APLYSPSYNN TNLLYNFSYN ANPFEFWVTR KSDGEVLFDT RGQKLVFEDQ
YIELTTNMVE NYNLYGLAET IHGLRLGNNL TRTFWANDEP SPVDQNMYGS HPYYLEQRYK
ADGINSTLNE TTYTSSSHGV LMLTANGMDV LLRQDYLQYR MIGGVIDLFV YSGSTESPKE
TVKQFVQSIG KPAMHQYWTL GYHSCRWGYT NITEIMDVRQ NYIDADIPVE TFWSDIDYME
KYRDFTVDPV SYSKSDMQTF FSDLVSNHQH YVPIIDAAIY AANPYNHTDD SYYPYYAGVE
KDIFLKNPNG SIYIGAVWPG FTAFPDFTNP DVVDYWKDCL INLTYAFGSN GTVPFSGIWT
DMNEPSSFCV GSCGSAMIDL NPAEPLTGIS KQYSIPEGFN VSNVTEYSSA YSASLSNYYA
TATSSVFQIV SPTATPLGLK PDYNIDWPPY AINNEQGNHD IANHIVSPNA TTHDGTQRYD
IFNMYGYGET KVSYAALTQI SPNERPFILS RSTFLGSGVY GAHWLGDNHS LWSNMFFSIS
GMIVFNMMGI PMVGADVCGF LGDSDEELCS RWMAMGAFSP FYRNHNNIYQ ISQEPYTWSS
VAEASRRAMY IRYSLLPYWY TIMAKASQDG TPALRALFVE FPNDPTLADV DRQFMVGDSL
LVTPVLEPNV EYVQGVFPGD NSTVWYDWYN HTEIVRQYNE NVTLYAPLEH INVAIRGGSV
LPMQQPSLTT YESRQNPFNL LVALDRDGSA TGELYLDDGV SIELNATLSV SFTFSDGVLS
AVPTGSYEVS QPLANVTILG LTESPSSITL NGQNVSSFQY SNDTEELLIT GLQNITSSGA
FANSWNLTL


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