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Reviewed, UniProtKB/Swiss-Prot P80072 (MALT_BACTQ)

Last modified May 5, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Maltase
    EC=3.2.1.20
Alternative name(s):
    Alpha-glucosidase I
OrganismBacillus thermoamyloliquefaciens
Taxonomic identifier1425 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›15Maltase
PRO_0000054326

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P80072-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 62B4CE501F2D3042

FASTA151,929
        10 
MKKAWWKEGV VYQIY 

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References

[1]"Assignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition."
Suzuki Y., Yonezawa K., Hattori M., Takii Y.
Eur. J. Biochem. 205:249-256(1992) [PubMed: 1555585] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: KP1071 / FERM P8477.

Cross-references

Sequence databases

PIRS21240.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Enzyme and pathway databases

BRENDA3.2.1.20. 288695.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameMALT_BACTQ
AccessionPrimary (citable) accession number: P80072
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 5, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents