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Reviewed, UniProtKB/Swiss-Prot Q9C0Y4 (AGLU_SCHPO)

Last modified November 25, 2008. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [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.

Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processoligosaccharide catabolic process

Inferred by curator. Source: GeneDB_SPombe

   Cellular componentextracellular region Ref.1

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-glucosidase activity Ref.1

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
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
Mutagenesis2871D → N: No loss of activity
Mutagenesis3551D → E or N: Almost total loss of activity
Mutagenesis4811D → A, E or N: Loss of activity
Mutagenesis4841E → A or Q: Loss of activity
Mutagenesis4841E → D: No loss of activity
Mutagenesis6471D → A, E or N: Loss of activity
Mutagenesis6761D → N: No loss of activity
Mutagenesis7141E → Q: No loss of activity
Mutagenesis8771D → N: Almost total loss of activity
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
Q9C0Y4-1 [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: 11298744] [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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAC36906.1.
AB045751 mRNA. Translation: BAB43946.1.
RefSeqNP_593996.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2543499.
KEGGspo:SPAPB24D3.10c.

Organism-specific databases

GeneDB_SpombeSPAPB24D3.10c.

Gene expression databases

ArrayExpressQ9C0Y4.

Family and domain databases

InterProIPR000322. Glyco_hydro_31.
[Graphical view]
PANTHERPTHR22762. Glyco_hydro_31. 1 hit.
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: November 25, 2008
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents