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Protein

Alpha-glucosidase

Gene

mal1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 sitei212 – 2121NucleophileBy similarity
Active sitei269 – 2691Proton donorBy similarity
Sitei346 – 3461Transition state stabilizerBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: UniProtKB-EC
  2. cation binding Source: InterPro
  3. dextrin alpha-glucosidase activity Source: PomBase
  4. maltose alpha-glucosidase activity Source: PomBase
  5. starch alpha-glucosidase activity Source: PomBase
  6. sucrose alpha-glucosidase activity Source: PomBase

GO - Biological processi

  1. cellular polysaccharide catabolic process Source: PomBase
  2. extracellular polysaccharide metabolic process Source: PomBase
  3. maltose metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Maltose metabolism

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Alternative name(s):
Maltase
Gene namesi
Name:mal1
ORF Names:SPBC1683.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC1683.07.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: PomBase
  2. cytosol Source: PomBase
  3. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Alpha-glucosidasePRO_0000310319Add
BLAST

Proteomic databases

MaxQBiQ9P6J3.

Expressioni

Inductioni

Repressed by glucose and inositol.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi276520. 8 interactions.
MINTiMINT-4704100.
STRINGi4896.SPBC1683.07-1.

Structurei

3D structure databases

ProteinModelPortaliQ9P6J3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000220641.
InParanoidiQ9P6J3.
KOiK01187.
OMAiRGHAANW.
OrthoDBiEOG7M3J7X.
PhylomeDBiQ9P6J3.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P6J3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVPSEKIK PNWWRETSVY QIYPASFKDS NGDGFGDLEG IISKVDYLKA
60 70 80 90 100
LNVESIWLCP IYPSPLKDMG YDVSDYKQID SRYGTLEDLD RLMKALHERD
110 120 130 140 150
MKLVMDLVLN HTSDQHEWFK ESRSSKTNPK RDWYFWKPAR YNEKGERLPP
160 170 180 190 200
NNWRSYFDTS AWEWDEATQE YYLHLWSVGQ PDLNWETPKV REAVHDILRF
210 220 230 240 250
WLDRGVDGFR LDAINMISKD QRFLDAPITD DRYEYQLAYQ YYANGPRIHE
260 270 280 290 300
YLNGIGNILT EYDAFSVGEM PYVLDTNEIL HVVGADRREL TMIFQFDFVD
310 320 330 340 350
LDLDPNQHKY IEGSWELSDL KKSLKKWQSA LLSGGGWNAS FIENHDQTRT
360 370 380 390 400
VSRYLSDSPK YRAYSSKLMA LFIIFQSGTP FVFQGQELAL ANIPRDWPID
410 420 430 440 450
EYLDVETQNF WKLFMSGNPS QEEIEKTMDI VNKRARDNGR TPMHWDSSPN
460 470 480 490 500
GGFTKAGVKP WMRVTNDYKE WNAANQVNDP ESPYTFWSKA LELRKELKDA
510 520 530 540 550
VVYGSFELIS EEDPSIVAFV RESSTYKLII LLNFTGNKVS YDCPLNLTSY
560 570
EILLDNYKDF ICMTSPVTLN PYQAVLLKL
Length:579
Mass (Da):67,752
Last modified:October 1, 2000 - v1
Checksum:i7B79064326E445AA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811F → L in AAY57566 (PubMed:16967902).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ019991 Genomic DNA. Translation: AAY57566.1.
CU329671 Genomic DNA. Translation: CAB91169.1.
RefSeqiNP_595063.1. NM_001020969.2.

Genome annotation databases

EnsemblFungiiSPBC1683.07.1; SPBC1683.07.1:pep; SPBC1683.07.
GeneIDi2539976.
KEGGispo:SPBC1683.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ019991 Genomic DNA. Translation: AAY57566.1.
CU329671 Genomic DNA. Translation: CAB91169.1.
RefSeqiNP_595063.1. NM_001020969.2.

3D structure databases

ProteinModelPortaliQ9P6J3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276520. 8 interactions.
MINTiMINT-4704100.
STRINGi4896.SPBC1683.07-1.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

MaxQBiQ9P6J3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1683.07.1; SPBC1683.07.1:pep; SPBC1683.07.
GeneIDi2539976.
KEGGispo:SPBC1683.07.

Organism-specific databases

PomBaseiSPBC1683.07.

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000220641.
InParanoidiQ9P6J3.
KOiK01187.
OMAiRGHAANW.
OrthoDBiEOG7M3J7X.
PhylomeDBiQ9P6J3.

Miscellaneous databases

NextBioi20801119.
PROiQ9P6J3.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of MAL1+ gene expression encoding maltase in Schizosaccharomyces pombe by added inositol."
    Yao S., Chi Z., He S.
    Indian J. Biochem. Biophys. 43:143-147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], REPRESSION BY GLUCOSE AND INOSITOL.
  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 nameiMALT_SCHPO
AccessioniPrimary (citable) accession number: Q9P6J3
Secondary accession number(s): Q4U125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.