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Protein

Alpha-glucosidase

Gene

agl1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei481Nucleophile1
Active sitei4841
Active sitei647Proton donor1

GO - Molecular functioni

  • alpha-1,4-glucosidase activity Source: UniProtKB-EC
  • carbohydrate binding Source: InterPro
  • maltose alpha-glucosidase activity Source: PomBase
  • starch alpha-glucosidase activity Source: PomBase

GO - Biological processi

  • maltose catabolic process Source: PomBase
  • oligosaccharide catabolic process Source: PomBase

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.20. 5613.
ReactomeiR-SPO-189085. Digestion of dietary carbohydrate.
R-SPO-6798695. Neutrophil degranulation.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Alternative name(s):
Maltase
Gene namesi
Name:agl1
Synonyms:agl
ORF Names:SPAPB24D3.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAPB24D3.10c. agl1.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: PomBase

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi218D → N: Almost total loss of activity. 1 Publication1
Mutagenesisi287D → N: No loss of activity. 1 Publication1
Mutagenesisi355D → E or N: Almost total loss of activity. 1 Publication1
Mutagenesisi481D → A, E or N: Loss of activity. 1 Publication1
Mutagenesisi484E → A or Q: Loss of activity. 1 Publication1
Mutagenesisi484E → D: No loss of activity. 1 Publication1
Mutagenesisi647D → A, E or N: Loss of activity. 1 Publication1
Mutagenesisi676D → N: No loss of activity. 1 Publication1
Mutagenesisi714E → Q: No loss of activity. 1 Publication1
Mutagenesisi877D → N: Almost total loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3784909.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001858125 – 969Alpha-glucosidaseAdd BLAST945

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi37N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi67N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi116N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi139N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi146N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi209N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi245N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi249N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi331N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi429N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi462N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi470N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi520N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi523N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi589N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi648N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi801N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi810N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi821N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi885N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi915N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi934N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi942N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi954N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi966N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9C0Y4.
PRIDEiQ9C0Y4.

Interactioni

Protein-protein interaction databases

MINTiMINT-4702058.
STRINGi4896.SPAPB24D3.10c.1.

Structurei

3D structure databases

ProteinModelPortaliQ9C0Y4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000041175.
InParanoidiQ9C0Y4.
OrthoDBiEOG092C0F23.
PhylomeDBiQ9C0Y4.

Family and domain databases

InterProiView protein in InterPro
IPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 1 hit.
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiView protein in PROSITE
PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9C0Y4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMISTAYQSL FLTALFSAIS IAVGNVYQTL NVIGDRNVTI PTNGIPQRLS
60 70 80 90 100
VYDPYRGVNC QGYQAVNISE SQNGVTAYLA LLGEPCYAYG TDYPLLFLNV
110 120 130 140 150
TYEEADRVHI SIKDANNTQF QFTSRKDLWD APLYSPSYNN TNLLYNFSYN
160 170 180 190 200
ANPFEFWVTR KSDGEVLFDT RGQKLVFEDQ YIELTTNMVE NYNLYGLAET
210 220 230 240 250
IHGLRLGNNL TRTFWANDEP SPVDQNMYGS HPYYLEQRYK ADGINSTLNE
260 270 280 290 300
TTYTSSSHGV LMLTANGMDV LLRQDYLQYR MIGGVIDLFV YSGSTESPKE
310 320 330 340 350
TVKQFVQSIG KPAMHQYWTL GYHSCRWGYT NITEIMDVRQ NYIDADIPVE
360 370 380 390 400
TFWSDIDYME KYRDFTVDPV SYSKSDMQTF FSDLVSNHQH YVPIIDAAIY
410 420 430 440 450
AANPYNHTDD SYYPYYAGVE KDIFLKNPNG SIYIGAVWPG FTAFPDFTNP
460 470 480 490 500
DVVDYWKDCL INLTYAFGSN GTVPFSGIWT DMNEPSSFCV GSCGSAMIDL
510 520 530 540 550
NPAEPLTGIS KQYSIPEGFN VSNVTEYSSA YSASLSNYYA TATSSVFQIV
560 570 580 590 600
SPTATPLGLK PDYNIDWPPY AINNEQGNHD IANHIVSPNA TTHDGTQRYD
610 620 630 640 650
IFNMYGYGET KVSYAALTQI SPNERPFILS RSTFLGSGVY GAHWLGDNHS
660 670 680 690 700
LWSNMFFSIS GMIVFNMMGI PMVGADVCGF LGDSDEELCS RWMAMGAFSP
710 720 730 740 750
FYRNHNNIYQ ISQEPYTWSS VAEASRRAMY IRYSLLPYWY TIMAKASQDG
760 770 780 790 800
TPALRALFVE FPNDPTLADV DRQFMVGDSL LVTPVLEPNV EYVQGVFPGD
810 820 830 840 850
NSTVWYDWYN HTEIVRQYNE NVTLYAPLEH INVAIRGGSV LPMQQPSLTT
860 870 880 890 900
YESRQNPFNL LVALDRDGSA TGELYLDDGV SIELNATLSV SFTFSDGVLS
910 920 930 940 950
AVPTGSYEVS QPLANVTILG LTESPSSITL NGQNVSSFQY SNDTEELLIT
960
GLQNITSSGA FANSWNLTL
Length:969
Mass (Da):108,686
Last modified:August 29, 2001 - v2
Checksum:iF3122E2CFA551C25
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30L → F in CAC36906 (PubMed:11859360).Curated1
Sequence conflicti220P → A in BAB43946 (PubMed:11298744).Curated1
Sequence conflicti507T → V in BAB43946 (PubMed:11298744).Curated1
Sequence conflicti566D → N in BAB43946 (PubMed:11298744).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36906.1.
AB045751 mRNA. Translation: BAB43946.1.

Similar proteinsi

Entry informationi

Entry nameiAGLU_SCHPO
AccessioniPrimary (citable) accession number: Q9C0Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: August 30, 2017
This is version 117 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families