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P00692 (AMY_BACAM) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-amylase
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifier1390 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length514 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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   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

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 3131 Ref.4
Chain32 – 514483Alpha-amylase
PRO_0000001330

Sites

Active site2621Nucleophile
Active site2921Proton donor
Metal binding1331Calcium 1
Metal binding1901Calcium 2
Metal binding1901Sodium
Metal binding2121Calcium 2; via carbonyl oxygen
Metal binding2141Calcium 2
Metal binding2141Sodium
Metal binding2251Calcium 1
Metal binding2251Sodium
Metal binding2311Calcium 1
Metal binding2311Sodium
Metal binding2331Calcium 2
Metal binding2351Calcium 2
Metal binding2661Calcium 1; via carbonyl oxygen
Metal binding3311Calcium 3; via carbonyl oxygen
Metal binding4381Calcium 3 By similarity
Metal binding4611Calcium 3 By similarity
Site3591Transition state stabilizer By similarity

Experimental info

Sequence conflict541L → I AA sequence Ref.4
Sequence conflict641I → L AA sequence Ref.4
Sequence conflict791S → D AA sequence Ref.4
Sequence conflict841G → S AA sequence Ref.4

Secondary structure

1 ......................................................................................... 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00692 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 3DE66B3FB5CCDE7E

FASTA51458,403
        10         20         30         40         50         60 
MIQKRKRTVS FRLVLMCTLL FVSLPITKTS AVNGTLMQYF EWYTPNDGQH WKRLQNDAEH 

        70         80         90        100        110        120 
LSDIGITAVW IPPAYKGLSQ SDNGYGPYDL YDLGEFQQKG TVRTKYGTKS ELQDAIGSLH 

       130        140        150        160        170        180 
SRNVQVYGDV VLNHKAGADA TEDVTAVEVN PANRNQETSE EYQIKAWTDF RFPGRGNTYS 

       190        200        210        220        230        240 
DFKWHWYHFD GADWDESRKI SRIFKFRGEG KAWDWEVSSE NGNYDYLMYA DVDYDHPDVV 

       250        260        270        280        290        300 
AETKKWGIWY ANELSLDGFR IDAAKHIKFS FLRDWVQAVR QATGKEMFTV AEYWQNNAGK 

       310        320        330        340        350        360 
LENYLNKTSF NQSVFDVPLH FNLQAASSQG GGYDMRRLLD GTVVSRHPEK AVTFVENHDT 

       370        380        390        400        410        420 
QPGQSLESTV QTWFKPLAYA FILTRESGYP QVFYGDMYGT KGTSPKEIPS LKDNIEPILK 

       430        440        450        460        470        480 
ARKEYAYGPQ HDYIDHPDVI GWTREGDSSA AKSGLAALIT DGPGGSKRMY AGLKNAGETW 

       490        500        510 
YDITGNRSDT VKIGSDGWGE FHVNDGSVSI YVQK

« Hide

References

[1]"Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene."
Takkinen K., Pettersson R.F., Kalkkinen N., Palva I., Soederlund H., Kaeaeriaeinen L.
J. Biol. Chem. 258:1007-1013(1983) [PubMed: 6185474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IH.
[2]"Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the alpha-amylase gene from Bacillus amyloliquefaciens."
Palva I., Pettersson R.F., Kalkkinen N., Lehtovaara P., Sarvas M., Soederlund H., Takkinen K., Kaeaeriaeinen L.
Gene 15:43-51(1981) [PubMed: 6170539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
[3]"Efficient secretion of Bacillus amyloliquefaciens alpha-amylase by its own signal peptide from Saccharomyces cerevisiae host cells."
Ruohonen L., Hackman P., Lehtovaara P., Knowles J.K.C., Karaenen S.
Gene 59:161-170(1987) [PubMed: 2830166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
[4]"Sequence of the N-terminal half of Bacillus amyloliquefaciens alpha-amylase."
Chung H.S., Friedberg F.
Biochem. J. 185:387-395(1980) [PubMed: 6156671] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-222.
[5]"Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes."
Brzozowski A.M., Lawson D.M., Turkenburg J.P., Bisgaard-Frantzen H., Svendsen A., Borchert T.V., Dauter Z., Wilson K.S., Davies G.J.
Biochemistry 39:9099-9107(2000) [PubMed: 10924103] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-331.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01542 mRNA. Translation: AAA22191.1.
V00092 Genomic DNA. Translation: CAA23430.1.
M18424 Genomic DNA. Translation: AAA22192.1.
PIRALBSN. A92389.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E3XX-ray1.90A32-513[»]
1E3ZX-ray1.93A32-513[»]
1E40X-ray2.20A32-513[»]
1E43X-ray1.70A32-513[»]
3BH4X-ray1.40A/B32-514[»]
ProteinModelPortalP00692.
SMRP00692. Positions 32-514.
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. 2 hits.
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_BACAM
AccessionPrimary (citable) accession number: P00692
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: December 14, 2011
This is version 100 of the entry and version 1 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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