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P06279 (AMY_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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-amylase
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:amyS
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 3 calcium ions per subunit.

Binds 1 sodium ion per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.1 Ref.5
Chain35 – 549515Alpha-amylase
PRO_0000001334

Sites

Active site2681Nucleophile
Active site2981Proton donor
Metal binding1391Calcium 1
Metal binding1961Calcium 2
Metal binding1961Sodium
Metal binding2181Calcium 2; via carbonyl oxygen
Metal binding2201Calcium 2
Metal binding2201Sodium
Metal binding2311Calcium 1
Metal binding2311Sodium
Metal binding2371Calcium 1
Metal binding2371Sodium
Metal binding2381Sodium; via carbonyl oxygen
Metal binding2391Calcium 2
Metal binding2721Calcium 1; via carbonyl oxygen
Metal binding3371Calcium 3; via carbonyl oxygen
Metal binding3391Calcium 3; via carbonyl oxygen
Metal binding4401Calcium 3; via carbonyl oxygen
Metal binding4411Calcium 3
Metal binding4641Calcium 3
Site3651Transition state stabilizer By similarity

Experimental info

Sequence conflict131M → V in AAA22241. Ref.3
Sequence conflict191L → W in AAA22241. Ref.3
Sequence conflict231L → S in CAA26547. Ref.2
Sequence conflict231L → S in AAA22241. Ref.3
Sequence conflict311P → H in CAA26547. Ref.2
Sequence conflict311P → H no nucleotide entry Ref.5
Sequence conflict1071A → T in CAA26547. Ref.2
Sequence conflict1071A → T in AAA22241. Ref.3
Sequence conflict1671T → I in AAA22227. Ref.4
Sequence conflict1791P → N in AAA22241. Ref.3
Sequence conflict2511S → N in CAA26547. Ref.2
Sequence conflict2511S → N in AAA22241. Ref.3
Sequence conflict260 – 2623TNI → RTL in AAA22227. Ref.4
Sequence conflict2841D → Y in CAA26547. Ref.2
Sequence conflict2841D → Y in AAA22241. Ref.3
Sequence conflict2841D → Y in AAA22227. Ref.4
Sequence conflict3121M → T in CAA26547. Ref.2
Sequence conflict3121M → T in AAA22241. Ref.3
Sequence conflict3381T → A in CAA26547. Ref.2
Sequence conflict3381T → A in AAA22241. Ref.3
Sequence conflict3421R → S in AAA22241. Ref.3
Sequence conflict3461T → N in AAA22241. Ref.3
Sequence conflict3761V → C in CAA26547. Ref.2
Sequence conflict526 – 5272WS → RP in CAA26547. Ref.2
Sequence conflict5271S → P in AAA22241. Ref.3
Sequence conflict5351D → G in CAA26547. Ref.2
Sequence conflict5351D → G in AAA22241. Ref.3

Secondary structure

1 ........................................................................................... 549
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06279 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 3A2DD93A955E79D3

FASTA54962,671
        10         20         30         40         50         60 
MLTFHRIIRK GWMFLLAFLL TALLFCPTGQ PAKAAAPFNG TMMQYFEWYL PDDGTLWTKV 

        70         80         90        100        110        120 
ANEANNLSSL GITALWLPPA YKGTSRSDVG YGVYDLYDLG EFNQKGAVRT KYGTKAQYLQ 

       130        140        150        160        170        180 
AIQAAHAAGM QVYADVVFDH KGGADGTEWV DAVEVNPSDR NQEISGTYQI QAWTKFDFPG 

       190        200        210        220        230        240 
RGNTYSSFKW RWYHFDGVDW DESRKLSRIY KFRGIGKAWD WEVDTENGNY DYLMYADLDM 

       250        260        270        280        290        300 
DHPEVVTELK SWGKWYVNTT NIDGFRLDAV KHIKFSFFPD WLSDVRSQTG KPLFTVGEYW 

       310        320        330        340        350        360 
SYDINKLHNY IMKTNGTMSL FDAPLHNKFY TASKSGGTFD MRTLMTNTLM KDQPTLAVTF 

       370        380        390        400        410        420 
VDNHDTEPGQ ALQSWVDPWF KPLAYAFILT RQEGYPCVFY GDYYGIPQYN IPSLKSKIDP 

       430        440        450        460        470        480 
LLIARRDYAY GTQHDYLDHS DIIGWTREGV TEKPGSGLAA LITDGPGGSK WMYVGKQHAG 

       490        500        510        520        530        540 
KVFYDLTGNR SDTVTINSDG WGEFKVNGGS VSVWVPRKTT VSTIAWSITT RPWTDEFVRW 


TEPRLVAWP

« Hide

References

[1]"Nucleotide sequence of the Bacillus stearothermophilus alpha-amylase gene."
Nakajima R., Imanaka T., Aiba S.
J. Bacteriol. 163:401-406(1985) [PubMed: 3924897] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-39.
[2]"Complete nucleotide sequence of a thermophilic alpha-amylase gene: homology between prokaryotic and eukaryotic alpha-amylases at the active sites."
Ihara H., Sasaki T., Tsuboi A., Yamagata H., Tsukagoshi N., Udaka S.
J. Biochem. 98:95-103(1985) [PubMed: 3876333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: DY5/PHI300.
[3]"Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis."
Gray G.L., Mainzer S.E., Rey M.W., Lamsa M.H., Kindle K.L., Carmona C., Requadt C.
J. Bacteriol. 166:635-643(1986) [PubMed: 3009417] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NZ-3.
[4]"Thermostable alpha amylase of Bacillus stearothermophilus: cloning, expression, and secretion by Escherichia coli."
Suominen I., Karp M., Lautamo J., Knowles J., Mantsaelae P.
(In) Chaloupka J., Krumphanzl V. (eds.); Extracellular enzymes of microorganisms, pp.129-137, Plenum Press, New York (1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Efficient synthesis and secretion of a thermophilic alpha-amylase by protein-producing Bacillus brevis 47 carrying the Bacillus stearothermophilus amylase gene."
Tsukagoshi N., Iritani S., Sasaki T., Takemura T., Ihara H., Idota Y., Yamagata H., Udaka S.
J. Bacteriol. 164:1182-1187(1985) [PubMed: 2999073] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122, PROTEIN SEQUENCE OF 35-48.
Strain: DY-5.
[6]"Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability."
Suvd D., Fujimoto Z., Takase K., Matsumura M., Mizuno H.
J. Biochem. 129:461-468(2001) [PubMed: 11226887] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M11450 Genomic DNA. Translation: AAA22235.2.
X02769 Genomic DNA. Translation: CAA26547.1.
M13255 Genomic DNA. Translation: AAA22241.1.
M57457 Genomic DNA. Translation: AAA22227.1.
PIRA24436.
ALBSF. A91999.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HVXX-ray2.00A35-549[»]
ProteinModelPortalP06279.
SMRP06279. Positions 35-517.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY_GEOSE
AccessionPrimary (citable) accession number: P06279
Secondary accession number(s): Q45519
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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