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Q02751 (MALT_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Maltase
Gene names
Name:MAL2
Synonyms:MAL1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Induction

By maltose and sucrose. Repressed by glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processMaltose metabolism
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processmaltose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncation binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 570569Alpha-glucosidase
PRO_0000054327

Sites

Active site2061Nucleophile By similarity
Active site2631Proton donor By similarity
Site3381Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02751 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F688281082968887

FASTA57066,210
        10         20         30         40         50         60 
MSEHKWWKEA VVYQIWPASY KDSNGDGVGD IPGIISTLDY IASLGVTTVW LSPMYDSPQD 

        70         80         90        100        110        120 
DMGYDVSDYE NVYSKYGTLQ DMDRLIAGCH DRGLKLILDL VINHTSVEHK WFKESRSSKD 

       130        140        150        160        170        180 
NPKRDWYIWK PPRIDSNGNK HPPNNWGSYF SGSAWKYDEL TGEYYLHLFA ESQPDLNWEN 

       190        200        210        220        230        240 
KECREAIYNS AIKFWLDKGV DGFRIDTAGM YSKYQHFKDA PVAFPDTEFQ PCEIYHKNGP 

       250        260        270        280        290        300 
RIHEFHKEMA KVMEPYDTMT VGEVGHSTRE QALKYVSAAE KEMNMMFLFD VVELGSDPRD 

       310        320        330        340        350        360 
RFRYNGFDLV DLKKAIKSQG EFAEGTDAWS TVFIENHDQA RAISRFGNDS PEFRVLSGKA 

       370        380        390        400        410        420 
IAMLQCCLTG TLFIYQGQEI GMTNVPRSWP IEEYKDINTI NYYRAFKEKY GKDADYKQKE 

       430        440        450        460        470        480 
EKLVDVINRL ARDNARTPVQ WSHQQYAGFS EVEPWMRVND NYKEINVEDQ DGDDHSLLNF 

       490        500        510        520        530        540 
YRKLLKLRGE YKDLFVYGEM KFLDFDDKKL FTFAKEAPGS PVAYIVINFS GEDVKFEPLI 

       550        560        570 
KGNYKLVLTN VDKDSKDALS PYEARMYVVD 

« Hide

References

[1]"Cloning and characterization of a Candida albicans maltase gene involved in sucrose utilization."
Geber A., Williamson P.R., Rex J.H., Sweeney E.C., Bennett J.E.
J. Bacteriol. 174:6992-6996(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-27.
Strain: ATCC 32354 / B311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94674 mRNA. Translation: AAA34350.2.
PIRA45249.

3D structure databases

ProteinModelPortalQ02751.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.
mycoCLAPAGL13B_CANAL.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0366.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMALT_CANAX
AccessionPrimary (citable) accession number: Q02751
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 78 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries