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P00691 (AMY_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 133. Feed History...

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

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:amyE
Synonyms:amyA
Ordered Locus Names:BSU03040
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length659 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 2 calcium ions 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
Complete proteome
Reference proteome
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: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Propeptide28 – 4114
PRO_0000001335
Chain42 – 659618Alpha-amylase
PRO_0000001336

Sites

Active site2171Nucleophile By similarity
Active site2491Proton donor By similarity
Metal binding1421Calcium 1
Metal binding1781Calcium 1; via carbonyl oxygen
Metal binding1871Calcium 1
Metal binding2101Calcium 2; via carbonyl oxygen
Metal binding2121Calcium 2
Metal binding2211Calcium 1; via carbonyl oxygen
Site3101Transition state stabilizer By similarity

Natural variations

Natural variant469 – 4779AKAPHVFLE → EMRCNTFFQ in strain: N7 AMYEN+.
Natural variant478 – 659182Missing in strain: N7 AMYEN+.

Experimental info

Sequence conflict221H → Y in CAA26086. Ref.2
Sequence conflict221H → Y in AAA22234. Ref.6
Sequence conflict221H → Y in CAA23436. Ref.7
Sequence conflict221H → Y in AAA22230. Ref.8
Sequence conflict1461S → F in CAA26086. Ref.2
Sequence conflict1461S → F in AAA22234. Ref.6
Sequence conflict2041D → E in CAA26086. Ref.2
Sequence conflict2041D → E in AAA22234. Ref.6
Sequence conflict2841N → K in CAA26086. Ref.2
Sequence conflict3321A → S in AAA22234. Ref.6
Sequence conflict513 – 52917ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in CAA23437. Ref.1
Sequence conflict513 – 52917ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in BAA08938. Ref.3

Secondary structure

............................................................................................. 659
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00691 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 16BD6CB1E7C67BD6

FASTA65972,378
        10         20         30         40         50         60 
MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG TILHAWNWSF 

        70         80         90        100        110        120 
NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY WLYQPTSYQI GNRYLGTEQE 

       130        140        150        160        170        180 
FKEMCAAAEE YGIKVIVDAV INHTTSDYAA ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN 

       190        200        210        220        230        240 
SLLGLYDWNT QNTQVQSYLK RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN 

       250        260        270        280        290        300 
TSAEFQYGEI LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD 

       310        320        330        340        350        360 
KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK 

       370        380        390        400        410        420 
SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN QIFMNQRGSH GVVLANAGSS 

       430        440        450        460        470        480 
SVSINTATKL PDGRYDNKAG AGSFQVNDGK LTGTINARSV AVLYPDDIAK APHVFLENYK 

       490        500        510        520        530        540 
TGVTHSFNDQ LTITLRADAN TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG 

       550        560        570        580        590        600 
TNSDGVTRTE KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM 

       610        620        630        640        650 
TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND SGLSGSLPH 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the amylase gene from Bacillus subtilis."
Yang M., Galizzi A., Henner D.J.
Nucleic Acids Res. 11:237-249(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Changes in the properties and molecular weights of Bacillus subtilis M-type and N-type alpha-amylases resulting from a spontaneous deletion."
Yamane K., Hirata Y., Furusato T., Yamazaki H., Nakayama A.
J. Biochem. 96:1849-1858(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: N7 AMYEN+.
[3]"The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
Yamane K., Kumano M., Kurita K.
Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 513-529.
[6]"Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences."
Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M., Tamura G., Yamane K.
J. Bacteriol. 156:327-337(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-557.
[7]"Nucleotide sequence of the promoter and NH2-terminal signal peptide region of Bacillus subtilis alpha-amylase gene cloned in pUB110."
Ohmura K., Yamazaki H., Takeichi Y., Nakayama A., Otozai K., Yamane K., Yamasaki M., Tamura G.
Biochem. Biophys. Res. Commun. 112:678-683(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
[8]"Molecular cloning and expression of an alpha-amylase gene from an alpha-amylase extrahyper producing Bacillus subtilis."
Emori M., Tojo T., Maruo B.
Agric. Biol. Chem. 52:399-406(1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
Strain: 168 / 2633.
[9]"Membrane-bound and soluble extracellular alpha-amylase from Bacillus subtilis."
Mantsala P., Zalkin H.
J. Biol. Chem. 254:8540-8547(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-58.
[10]"Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose."
Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T., Mizuno H.
J. Mol. Biol. 277:393-407(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 42-466.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00101 Genomic DNA. Translation: CAA23437.1.
V00100 Genomic DNA. Translation: CAA23436.1.
D50453 Genomic DNA. Translation: BAA08938.1.
AL009126 Genomic DNA. Translation: CAB12098.2.
K00563 Genomic DNA. Translation: AAA22234.1.
X02150 Genomic DNA. Translation: CAA26086.1.
M35517 Genomic DNA. Translation: AAA22230.1.
PIRALBS. A00842.
ALBSNA. A91793.
RefSeqNP_388186.2. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAGX-ray2.50A42-466[»]
1UA7X-ray2.21A45-466[»]
ProteinModelPortalP00691.
SMRP00691. Positions 42-466, 560-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU03040.

Protein family/group databases

CAZyCBM26. Carbohydrate-Binding Module Family 26.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbP00691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12098; CAB12098; BSU03040.
GeneID938356.
KEGGbsu:BSU03040.
PATRIC18972167. VBIBacSub10457_0312.

Organism-specific databases

GenoListBSU03040. [Micado]

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000008732.
KOK01176.
OrthoDBEOG6F55CH.

Enzyme and pathway databases

BioCycBSUB:BSU03040-MONOMER.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00691.

Entry information

Entry nameAMY_BACSU
AccessionPrimary (citable) accession number: P00691
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList