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Q9C0Y4 (AGLU_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Maltase
Gene names
Name:agl1
Synonyms:agl
ORF Names:SPAPB24D3.10c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length969 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.1
Chain25 – 969945Alpha-glucosidase
PRO_0000018581

Sites

Active site4811Nucleophile
Active site4841
Active site6471Proton donor

Amino acid modifications

Glycosylation371N-linked (GlcNAc...) Potential
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential
Glycosylation5891N-linked (GlcNAc...) Potential
Glycosylation6481N-linked (GlcNAc...) Potential
Glycosylation8011N-linked (GlcNAc...) Potential
Glycosylation8101N-linked (GlcNAc...) Potential
Glycosylation8211N-linked (GlcNAc...) Potential
Glycosylation8851N-linked (GlcNAc...) Potential
Glycosylation9151N-linked (GlcNAc...) Potential
Glycosylation9341N-linked (GlcNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Potential
Glycosylation9541N-linked (GlcNAc...) Potential
Glycosylation9661N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis2181D → N: Almost total loss of activity. Ref.1
Mutagenesis2871D → N: No loss of activity. Ref.1
Mutagenesis3551D → E or N: Almost total loss of activity. Ref.1
Mutagenesis4811D → A, E or N: Loss of activity. Ref.1
Mutagenesis4841E → A or Q: Loss of activity. Ref.1
Mutagenesis4841E → D: No loss of activity. Ref.1
Mutagenesis6471D → A, E or N: Loss of activity. Ref.1
Mutagenesis6761D → N: No loss of activity. Ref.1
Mutagenesis7141E → Q: No loss of activity. Ref.1
Mutagenesis8771D → N: Almost total loss of activity. Ref.1
Sequence conflict301L → F in CAC36906. Ref.2
Sequence conflict2201P → A in BAB43946. Ref.1
Sequence conflict5071T → V in BAB43946. Ref.1
Sequence conflict5661D → N in BAB43946. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9C0Y4 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: F3122E2CFA551C25

FASTA969108,686
        10         20         30         40         50         60 
MMISTAYQSL FLTALFSAIS IAVGNVYQTL NVIGDRNVTI PTNGIPQRLS VYDPYRGVNC 

        70         80         90        100        110        120 
QGYQAVNISE SQNGVTAYLA LLGEPCYAYG TDYPLLFLNV TYEEADRVHI SIKDANNTQF 

       130        140        150        160        170        180 
QFTSRKDLWD APLYSPSYNN TNLLYNFSYN ANPFEFWVTR KSDGEVLFDT RGQKLVFEDQ 

       190        200        210        220        230        240 
YIELTTNMVE NYNLYGLAET IHGLRLGNNL TRTFWANDEP SPVDQNMYGS HPYYLEQRYK 

       250        260        270        280        290        300 
ADGINSTLNE TTYTSSSHGV LMLTANGMDV LLRQDYLQYR MIGGVIDLFV YSGSTESPKE 

       310        320        330        340        350        360 
TVKQFVQSIG KPAMHQYWTL GYHSCRWGYT NITEIMDVRQ NYIDADIPVE TFWSDIDYME 

       370        380        390        400        410        420 
KYRDFTVDPV SYSKSDMQTF FSDLVSNHQH YVPIIDAAIY AANPYNHTDD SYYPYYAGVE 

       430        440        450        460        470        480 
KDIFLKNPNG SIYIGAVWPG FTAFPDFTNP DVVDYWKDCL INLTYAFGSN GTVPFSGIWT 

       490        500        510        520        530        540 
DMNEPSSFCV GSCGSAMIDL NPAEPLTGIS KQYSIPEGFN VSNVTEYSSA YSASLSNYYA 

       550        560        570        580        590        600 
TATSSVFQIV SPTATPLGLK PDYNIDWPPY AINNEQGNHD IANHIVSPNA TTHDGTQRYD 

       610        620        630        640        650        660 
IFNMYGYGET KVSYAALTQI SPNERPFILS RSTFLGSGVY GAHWLGDNHS LWSNMFFSIS 

       670        680        690        700        710        720 
GMIVFNMMGI PMVGADVCGF LGDSDEELCS RWMAMGAFSP FYRNHNNIYQ ISQEPYTWSS 

       730        740        750        760        770        780 
VAEASRRAMY IRYSLLPYWY TIMAKASQDG TPALRALFVE FPNDPTLADV DRQFMVGDSL 

       790        800        810        820        830        840 
LVTPVLEPNV EYVQGVFPGD NSTVWYDWYN HTEIVRQYNE NVTLYAPLEH INVAIRGGSV 

       850        860        870        880        890        900 
LPMQQPSLTT YESRQNPFNL LVALDRDGSA TGELYLDDGV SIELNATLSV SFTFSDGVLS 

       910        920        930        940        950        960 
AVPTGSYEVS QPLANVTILG LTESPSSITL NGQNVSSFQY SNDTEELLIT GLQNITSSGA 


FANSWNLTL 

« Hide

References

« Hide 'large scale' references
[1]"Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of alpha-glucosidase from Schizosaccharomyces pombe."
Okuyama M., Okuno A., Shimizu N., Mori H., Kimura A., Chiba S.
Eur. J. Biochem. 268:2270-2280(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36; 175-194; 375-395 AND 427-451, MUTAGENESIS OF ASP-218; ASP-287; ASP-355; ASP-481; GLU-484; ASP-647; ASP-676; GLU-714 AND ASP-877.
[2]"The genome sequence of Schizosaccharomyces pombe."
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. expand/collapse author list , 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.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAC36906.1.
AB045751 mRNA. Translation: BAB43946.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4702058.
STRING4896.SPAPB24D3.10c-1.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.
mycoCLAPAGL31A_SCHPO.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

PomBaseSPAPB24D3.10c.

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000041175.
OrthoDBEOG77T1CZ.
PhylomeDBQ9C0Y4.

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804509.

Entry information

Entry nameAGLU_SCHPO
AccessionPrimary (citable) accession number: Q9C0Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries