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Q9C0Y4

- AGLU_SCHPO

UniProt

Q9C0Y4 - AGLU_SCHPO

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Protein

Alpha-glucosidase

Gene

agl1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei481 – 4811Nucleophile
Active sitei484 – 4841
Active sitei647 – 6471Proton donor

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: PomBase
  2. carbohydrate binding Source: InterPro
  3. maltose alpha-glucosidase activity Source: PomBase
  4. starch alpha-glucosidase activity Source: PomBase

GO - Biological processi

  1. cellular polysaccharide catabolic process Source: PomBase
  2. maltose catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31A_SCHPO.

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
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAPB24D3.10c.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi218 – 2181D → N: Almost total loss of activity. 1 Publication
Mutagenesisi287 – 2871D → N: No loss of activity. 1 Publication
Mutagenesisi355 – 3551D → E or N: Almost total loss of activity. 1 Publication
Mutagenesisi481 – 4811D → A, E or N: Loss of activity. 1 Publication
Mutagenesisi484 – 4841E → A or Q: Loss of activity. 1 Publication
Mutagenesisi484 – 4841E → D: No loss of activity. 1 Publication
Mutagenesisi647 – 6471D → A, E or N: Loss of activity. 1 Publication
Mutagenesisi676 – 6761D → N: No loss of activity. 1 Publication
Mutagenesisi714 – 7141E → Q: No loss of activity. 1 Publication
Mutagenesisi877 – 8771D → N: Almost total loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 969945Alpha-glucosidasePRO_0000018581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi589 – 5891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi648 – 6481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi821 – 8211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi915 – 9151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi934 – 9341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi954 – 9541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi966 – 9661N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9C0Y4.

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

eggNOGiCOG1501.
HOGENOMiHOG000041175.
InParanoidiQ9C0Y4.
OrthoDBiEOG77T1CZ.
PhylomeDBiQ9C0Y4.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301L → F in CAC36906. (PubMed:11859360)Curated
Sequence conflicti220 – 2201P → A in BAB43946. (PubMed:11298744)Curated
Sequence conflicti507 – 5071T → V in BAB43946. (PubMed:11298744)Curated
Sequence conflicti566 – 5661D → N in BAB43946. (PubMed:11298744)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAC36906.1.
AB045751 mRNA. Translation: BAB43946.1.

Genome annotation databases

EnsemblFungiiSPAPB24D3.10c.1; SPAPB24D3.10c.1:pep; SPAPB24D3.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAC36906.1 .
AB045751 mRNA. Translation: BAB43946.1 .

3D structure databases

ProteinModelPortali Q9C0Y4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4702058.
STRINGi 4896.SPAPB24D3.10c-1.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.
mycoCLAPi AGL31A_SCHPO.

Proteomic databases

MaxQBi Q9C0Y4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAPB24D3.10c.1 ; SPAPB24D3.10c.1:pep ; SPAPB24D3.10c .

Organism-specific databases

PomBasei SPAPB24D3.10c.

Phylogenomic databases

eggNOGi COG1501.
HOGENOMi HOG000041175.
InParanoidi Q9C0Y4.
OrthoDBi EOG77T1CZ.
PhylomeDBi Q9C0Y4.

Miscellaneous databases

NextBioi 20804509.

Family and domain databases

InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF01055. Glyco_hydro_31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAGLU_SCHPO
AccessioniPrimary (citable) accession number: Q9C0Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: October 29, 2014
This is version 98 of the entry and version 2 of the sequence. [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

External Data

Dasty 3