AGLU_SCHPO
ID AGLU_SCHPO Reviewed; 969 AA.
AC Q9C0Y4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Alpha-glucosidase;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
DE Flags: Precursor;
GN Name=agl1; Synonyms=agl; ORFNames=SPAPB24D3.10c;
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 [MRNA], PROTEIN SEQUENCE OF 25-36; 175-194; 375-395 AND
RP 427-451, AND MUTAGENESIS OF ASP-218; ASP-287; ASP-355; ASP-481; GLU-484;
RP ASP-647; ASP-676; GLU-714 AND ASP-877.
RX PubMed=11298744; DOI=10.1046/j.1432-1327.2001.02104.x;
RA Okuyama M., Okuno A., Shimizu N., Mori H., Kimura A., Chiba S.;
RT "Carboxyl group of residue Asp647 as possible proton donor in catalytic
RT reaction of alpha-glucosidase from Schizosaccharomyces pombe.";
RL Eur. J. Biochem. 268:2270-2280(2001).
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 -!- FUNCTION: Hydrolyzes malto-oligosaccharides, but has a low activity
CC toward soluble starch.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; CU329670; CAC36906.1; -; Genomic_DNA.
DR EMBL; AB045751; BAB43946.1; -; mRNA.
DR RefSeq; NP_593996.1; NM_001019422.2.
DR AlphaFoldDB; Q9C0Y4; -.
DR SMR; Q9C0Y4; -.
DR STRING; 4896.SPAPB24D3.10c.1; -.
DR ChEMBL; CHEMBL3784909; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR MaxQB; Q9C0Y4; -.
DR PaxDb; Q9C0Y4; -.
DR GeneID; 2543499; -.
DR KEGG; spo:SPAPB24D3.10c; -.
DR PomBase; SPAPB24D3.10c; agl1.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR InParanoid; Q9C0Y4; -.
DR PhylomeDB; Q9C0Y4; -.
DR BRENDA; 3.2.1.20; 5613.
DR Reactome; R-SPO-189085; Digestion of dietary carbohydrate.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:Q9C0Y4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005576; C:extracellular region; IDA:PomBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0044654; F:starch alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0000025; P:maltose catabolic process; IDA:PomBase.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; EXP:PomBase.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:11298744"
FT CHAIN 25..969
FT /note="Alpha-glucosidase"
FT /id="PRO_0000018581"
FT ACT_SITE 481
FT /note="Nucleophile"
FT ACT_SITE 484
FT ACT_SITE 647
FT /note="Proton donor"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 218
FT /note="D->N: Almost total loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 287
FT /note="D->N: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 355
FT /note="D->E,N: Almost total loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 481
FT /note="D->A,E,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 484
FT /note="E->A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 484
FT /note="E->D: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 647
FT /note="D->A,E,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 676
FT /note="D->N: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 714
FT /note="E->Q: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT MUTAGEN 877
FT /note="D->N: Almost total loss of activity."
FT /evidence="ECO:0000269|PubMed:11298744"
FT CONFLICT 30
FT /note="L -> F (in Ref. 2; CAC36906)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="P -> A (in Ref. 1; BAB43946)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="T -> V (in Ref. 1; BAB43946)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="D -> N (in Ref. 1; BAB43946)"
FT /evidence="ECO:0000305"
SQ 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
