Alpha-glucosidase precursor - Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

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Q9C0Y4 (AGLU_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-glucosidase
EC=3.2.1.20

Alternative name(s):
Maltase

Gene names

Name:	agl1
Synonyms:	agl
ORF Names:	SPAPB24D3.10c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	969 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular polysaccharide catabolic process Inferred by curator. Source: GeneDB_Spombe oligosaccharide catabolic process Inferred by curator. Source: GeneDB_Spombe
Cellular component	extracellular region Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro maltose alpha-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

24

Chain

945

Alpha-glucosidase

PRO_0000018581

Sites

Active site

1

Nucleophile

Active site

1

Active site

1

Proton donor

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

1

D → N: Almost total loss of activity. Ref.1

Mutagenesis

1

D → N: No loss of activity. Ref.1

Mutagenesis

1

D → E or N: Almost total loss of activity. Ref.1

Mutagenesis

1

D → A, E or N: Loss of activity. Ref.1

Mutagenesis

1

E → A or Q: Loss of activity. Ref.1

Mutagenesis

1

E → D: No loss of activity. Ref.1

Mutagenesis

1

D → A, E or N: Loss of activity. Ref.1

Mutagenesis

1

D → N: No loss of activity. Ref.1

Mutagenesis

1

E → Q: No loss of activity. Ref.1

Mutagenesis

1

D → N: Almost total loss of activity. Ref.1

Sequence conflict

1

L → F in CAC36906. Ref.2

Sequence conflict

1

P → A in BAB43946. Ref.1

Sequence conflict

1

T → V in BAB43946. Ref.1

Sequence conflict

1

D → N in BAB43946. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9C0Y4 [UniParc].

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

969

108,686

        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

References

	« Hide 'large scale' referencesShow '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. Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC36906.1. AB045751 mRNA. Translation: BAB43946.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9C0Y4.
Protein family/group databases
CAZy	GH31. Glycoside Hydrolase Family 31.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GenomeReviews	Gene locus agl1 in contig CU329670_GR.
Organism-specific databases
GeneDB_Spombe	SPAPB24D3.10c.
Phylogenomic databases
eggNOG	fuNOG06435.
GeneTree	EFGT00050000002321.
HOGENOM	HBG738610.
OrthoDB	EOG4J40R4.
Gene expression databases
ArrayExpress	Q9C0Y4.
Family and domain databases
InterPro	IPR011013. Glyco_hydro-type_carb-bd. IPR000322. Glyco_hydro_31. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR22762. Glyco_hydro_31. 1 hit.
Pfam	PF01055. Glyco_hydro_31. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit. PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGLU_SCHPO

Accession

Primary (citable) accession number: Q9C0Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	August 29, 2001
Last modified:	December 14, 2011
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents