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Protein

Alpha-amylase

Gene

amyE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi142 – 1421Calcium 1
Metal bindingi178 – 1781Calcium 1; via carbonyl oxygen
Metal bindingi187 – 1871Calcium 1
Metal bindingi210 – 2101Calcium 2; via carbonyl oxygen
Metal bindingi212 – 2121Calcium 2
Active sitei217 – 2171NucleophileBy similarity
Metal bindingi221 – 2211Calcium 1; via carbonyl oxygen
Active sitei249 – 2491Proton donorBy similarity
Sitei310 – 3101Transition state stabilizerBy similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU03040-MONOMER.

Protein family/group databases

CAZyiCBM26. Carbohydrate-Binding Module Family 26.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:amyE
Synonyms:amyA
Ordered Locus Names:BSU03040
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU03040. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Propeptidei28 – 4114PRO_0000001335Add
BLAST
Chaini42 – 659618Alpha-amylasePRO_0000001336Add
BLAST

Proteomic databases

PaxDbiP00691.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi224308.BSU03040.

Structurei

Secondary structure

1
659
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni47 – 493Combined sources
Beta strandi52 – 543Combined sources
Helixi60 – 656Combined sources
Helixi67 – 726Combined sources
Beta strandi76 – 805Combined sources
Beta strandi84 – 863Combined sources
Helixi90 – 923Combined sources
Helixi96 – 1038Combined sources
Beta strandi105 – 1128Combined sources
Turni113 – 1153Combined sources
Helixi118 – 12912Combined sources
Turni130 – 1323Combined sources
Beta strandi134 – 1396Combined sources
Turni148 – 1503Combined sources
Helixi153 – 1564Combined sources
Beta strandi162 – 1643Combined sources
Helixi174 – 1796Combined sources
Beta strandi180 – 1823Combined sources
Helixi193 – 20816Combined sources
Beta strandi213 – 2164Combined sources
Helixi219 – 2213Combined sources
Helixi228 – 2303Combined sources
Helixi234 – 2385Combined sources
Beta strandi244 – 2485Combined sources
Helixi258 – 2625Combined sources
Beta strandi265 – 2684Combined sources
Helixi270 – 28213Combined sources
Helixi287 – 2904Combined sources
Beta strandi294 – 2974Combined sources
Helixi299 – 3013Combined sources
Beta strandi302 – 3043Combined sources
Helixi309 – 3135Combined sources
Turni318 – 3214Combined sources
Helixi324 – 33512Combined sources
Beta strandi337 – 3459Combined sources
Beta strandi359 – 3613Combined sources
Helixi369 – 3724Combined sources
Helixi374 – 38613Combined sources
Helixi396 – 3983Combined sources
Beta strandi402 – 4076Combined sources
Turni408 – 4103Combined sources
Beta strandi411 – 4166Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi422 – 4276Combined sources
Beta strandi432 – 4365Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi450 – 4556Combined sources
Beta strandi459 – 4635Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAGX-ray2.50A42-466[»]
1UA7X-ray2.21A45-466[»]
ProteinModelPortaliP00691.
SMRiP00691. Positions 42-466, 560-650.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00691.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000008732.
InParanoidiP00691.
KOiK01176.
OMAiAYANYMN.
OrthoDBiEOG6F55CH.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00691-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG
60 70 80 90 100
TILHAWNWSF NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY
110 120 130 140 150
WLYQPTSYQI GNRYLGTEQE FKEMCAAAEE YGIKVIVDAV INHTTSDYAA
160 170 180 190 200
ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN SLLGLYDWNT QNTQVQSYLK
210 220 230 240 250
RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN TSAEFQYGEI
260 270 280 290 300
LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD
310 320 330 340 350
KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG
360 370 380 390 400
GGNGVRFPGK SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN
410 420 430 440 450
QIFMNQRGSH GVVLANAGSS SVSINTATKL PDGRYDNKAG AGSFQVNDGK
460 470 480 490 500
LTGTINARSV AVLYPDDIAK APHVFLENYK TGVTHSFNDQ LTITLRADAN
510 520 530 540 550
TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG TNSDGVTRTE
560 570 580 590 600
KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM
610 620 630 640 650
TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND

SGLSGSLPH
Length:659
Mass (Da):72,378
Last modified:June 16, 2009 - v2
Checksum:i16BD6CB1E7C67BD6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221H → Y in CAA26086 (PubMed:6099357).Curated
Sequence conflicti22 – 221H → Y in AAA22234 (PubMed:6413492).Curated
Sequence conflicti22 – 221H → Y in CAA23436 (PubMed:6189486).Curated
Sequence conflicti22 – 221H → Y in AAA22230 (Ref. 8) Curated
Sequence conflicti146 – 1461S → F in CAA26086 (PubMed:6099357).Curated
Sequence conflicti146 – 1461S → F in AAA22234 (PubMed:6413492).Curated
Sequence conflicti204 – 2041D → E in CAA26086 (PubMed:6099357).Curated
Sequence conflicti204 – 2041D → E in AAA22234 (PubMed:6413492).Curated
Sequence conflicti284 – 2841N → K in CAA26086 (PubMed:6099357).Curated
Sequence conflicti332 – 3321A → S in AAA22234 (PubMed:6413492).Curated
Sequence conflicti513 – 52917ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in CAA23437 (PubMed:6186986).CuratedAdd
BLAST
Sequence conflicti513 – 52917ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in BAA08938 (PubMed:8969502).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti469 – 4779AKAPHVFLE → EMRCNTFFQ in strain: N7 AMYEN+.
Natural varianti478 – 659182Missing in strain: N7 AMYEN+.
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA00842. ALBS.
A91793. ALBSNA.
RefSeqiNP_388186.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12098; CAB12098; BSU03040.
GeneIDi938356.
KEGGibsu:BSU03040.
PATRICi18972167. VBIBacSub10457_0312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA00842. ALBS.
A91793. ALBSNA.
RefSeqiNP_388186.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAGX-ray2.50A42-466[»]
1UA7X-ray2.21A45-466[»]
ProteinModelPortaliP00691.
SMRiP00691. Positions 42-466, 560-650.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU03040.

Protein family/group databases

CAZyiCBM26. Carbohydrate-Binding Module Family 26.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP00691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12098; CAB12098; BSU03040.
GeneIDi938356.
KEGGibsu:BSU03040.
PATRICi18972167. VBIBacSub10457_0312.

Organism-specific databases

GenoListiBSU03040. [Micado]

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000008732.
InParanoidiP00691.
KOiK01176.
OMAiAYANYMN.
OrthoDBiEOG6F55CH.

Enzyme and pathway databases

BioCyciBSUB:BSU03040-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00691.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAMY_BACSU
AccessioniPrimary (citable) accession number: P00691
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 16, 2009
Last modified: January 7, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.