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Reviewed, UniProtKB/Swiss-Prot P19571 (AMT6_BACS7)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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Names and origin

Protein namesRecommended name:
    Glucan 1,4-alpha-maltohexaosidase
    EC=3.2.1.98
Alternative name(s):
    G6-amylase
    Maltohexaose-producing amylase
    Exo-maltohexaohydrolase
OrganismBacillus sp. (strain 707)
Taxonomic identifier1416 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.

Cofactor

Binds 2 calcium ions per subunit By similarity.

Binds 1 sodium ion per subunit By similarity.

Pathway

Glycan degradation; starch degradation.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

glucan 1,4-alpha-maltohexaosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.1
Chain34 – 518485Glucan 1,4-alpha-maltohexaosidase
PRO_0000001421

Sites

Active site2691Nucleophile By similarity
Active site2991Proton donor By similarity
Active site3661 By similarity
Metal binding1391Calcium 1 By similarity
Metal binding1961Calcium 2 By similarity
Metal binding1961Sodium By similarity
Metal binding2191Calcium 2; via carbonyl oxygen By similarity
Metal binding2211Calcium 2 By similarity
Metal binding2211Sodium By similarity
Metal binding2321Calcium 1 By similarity
Metal binding2321Sodium By similarity
Metal binding2381Calcium 1 By similarity
Metal binding2381Sodium By similarity
Metal binding2401Calcium 2 By similarity
Metal binding2421Calcium 2 By similarity
Metal binding2731Calcium 1; via carbonyl oxygen By similarity

Secondary structure

1 .............................................................................................. 518
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P19571-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 3A961E21612682C4

FASTA51859,009
        10         20         30         40         50         60 
MKMRTGKKGF LSILLAFLLV ITSIPFTLVD VEAHHNGTNG TMMQYFEWYL PNDGNHWNRL 

        70         80         90        100        110        120 
NSDASNLKSK GITAVWIPPA WKGASQNDVG YGAYDLYDLG EFNQKGTVRT KYGTRSQLQA 

       130        140        150        160        170        180 
AVTSLKNNGI QVYGDVVMNH KGGADATEMV RAVEVNPNNR NQEVTGEYTI EAWTRFDFPG 

       190        200        210        220        230        240 
RGNTHSSFKW RWYHFDGVDW DQSRRLNNRI YKFRGHGKAW DWEVDTENGN YDYLMYADID 

       250        260        270        280        290        300 
MDHPEVVNEL RNWGVWYTNT LGLDGFRIDA VKHIKYSFTR DWINHVRSAT GKNMFAVAEF 

       310        320        330        340        350        360 
WKNDLGAIEN YLQKTNWNHS VFDVPLHYNL YNASKSGGNY DMRNIFNGTV VQRHPSHAVT 

       370        380        390        400        410        420 
FVDNHDSQPE EALESFVEEW FKPLAYALTL TREQGYPSVF YGDYYGIPTH GVPAMRSKID 

       430        440        450        460        470        480 
PILEARQKYA YGKQNDYLDH HNIIGWTREG NTAHPNSGLA TIMSDGAGGS KWMFVGRNKA 

       490        500        510 
GQVWSDITGN RTGTVTINAD GWGNFSVNGG SVSIWVNK

« Hide

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References

[1]"Nucleotide sequence of the maltohexaose-producing amylase gene from an alkalophilic Bacillus sp. #707 and structural similarity to liquefying type alpha-amylases."
Tsukamoto A., Kimura K., Ishii Y., Takano T., Yamane K.
Biochem. Biophys. Res. Commun. 151:25-31(1988) [PubMed: 3258152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-36.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M18862 Genomic DNA. Translation: AAA22231.1.
PIRA27705.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WP6X-ray2.10A34-518[»]
1WPCX-ray1.90A34-518[»]
2D3LX-ray2.30A34-518[»]
2D3NX-ray1.90A34-518[»]
2GJPX-ray1.90A34-516[»]
2GJRX-ray2.10A34-516[»]
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Family and domain databases

InterProIPR013776. A-amylase_thermo.
IPR006046. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFPIRSF001021. Alph-amls_thrmst. 1 hit.
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMT6_BACS7
AccessionPrimary (citable) accession number: P19571
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 16, 2009
This is version 69 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)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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