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Protein

Alpha-amylase

Gene

amyS

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit.1 Publication
  • Na+1 PublicationNote: Binds 1 sodium ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Calcium 1Combined sources1 Publication
Metal bindingi196 – 1961Calcium 2Combined sources1 Publication
Metal bindingi196 – 1961SodiumCombined sources1 Publication
Metal bindingi218 – 2181Calcium 2; via carbonyl oxygenCombined sources1 Publication
Metal bindingi220 – 2201Calcium 2Combined sources1 Publication
Metal bindingi220 – 2201SodiumCombined sources1 Publication
Metal bindingi231 – 2311Calcium 1Combined sources1 Publication
Metal bindingi231 – 2311SodiumCombined sources1 Publication
Metal bindingi237 – 2371Calcium 1Combined sources1 Publication
Metal bindingi237 – 2371SodiumCombined sources1 Publication
Metal bindingi238 – 2381Sodium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi239 – 2391Calcium 2Combined sources1 Publication
Active sitei268 – 2681Nucleophile
Metal bindingi272 – 2721Calcium 1; via carbonyl oxygenCombined sources1 Publication
Active sitei298 – 2981Proton donor
Metal bindingi337 – 3371Calcium 3; via carbonyl oxygenCombined sources1 Publication
Metal bindingi339 – 3391Calcium 3; via carbonyl oxygenCombined sources1 Publication
Sitei365 – 3651Transition state stabilizerBy similarity
Metal bindingi440 – 4401Calcium 3; via carbonyl oxygenCombined sources1 Publication
Metal bindingi441 – 4411Calcium 3Combined sources1 Publication
Metal bindingi464 – 4641Calcium 3Combined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.1. 623.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.11 Publication)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:amyS
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Secreted 2 Publications

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34342 PublicationsAdd
BLAST
Chaini35 – 549515Alpha-amylasePRO_0000001334Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Beta strandi52 – 543Combined sources
Helixi56 – 6914Combined sources
Beta strandi74 – 774Combined sources
Beta strandi81 – 855Combined sources
Beta strandi90 – 956Combined sources
Beta strandi107 – 1104Combined sources
Helixi115 – 12713Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi145 – 15612Combined sources
Beta strandi159 – 1635Combined sources
Beta strandi168 – 1769Combined sources
Turni179 – 1835Combined sources
Helixi192 – 1943Combined sources
Beta strandi195 – 2017Combined sources
Turni202 – 2054Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi234 – 2385Combined sources
Helixi243 – 26018Combined sources
Beta strandi264 – 2674Combined sources
Helixi270 – 2723Combined sources
Helixi277 – 28913Combined sources
Beta strandi294 – 2974Combined sources
Helixi304 – 31310Combined sources
Turni314 – 3163Combined sources
Beta strandi318 – 3214Combined sources
Helixi323 – 33311Combined sources
Turni334 – 3374Combined sources
Helixi341 – 3433Combined sources
Turni344 – 3474Combined sources
Helixi349 – 3524Combined sources
Helixi354 – 3563Combined sources
Beta strandi357 – 3615Combined sources
Turni364 – 3663Combined sources
Turni378 – 3803Combined sources
Helixi381 – 39010Combined sources
Beta strandi391 – 3999Combined sources
Helixi400 – 4045Combined sources
Helixi407 – 4093Combined sources
Helixi415 – 42713Combined sources
Beta strandi433 – 4364Combined sources
Beta strandi439 – 4479Combined sources
Beta strandi458 – 4658Combined sources
Beta strandi468 – 4736Combined sources
Helixi476 – 4783Combined sources
Beta strandi482 – 4854Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi500 – 5067Combined sources
Beta strandi511 – 5166Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HVXX-ray2.00A35-549[»]
4UZUX-ray1.90A35-549[»]
ProteinModelPortaliP06279.
SMRiP06279. Positions 35-517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06279.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P06279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTFHRIIRK GWMFLLAFLL TALLFCPTGQ PAKAAAPFNG TMMQYFEWYL
60 70 80 90 100
PDDGTLWTKV ANEANNLSSL GITALWLPPA YKGTSRSDVG YGVYDLYDLG
110 120 130 140 150
EFNQKGAVRT KYGTKAQYLQ AIQAAHAAGM QVYADVVFDH KGGADGTEWV
160 170 180 190 200
DAVEVNPSDR NQEISGTYQI QAWTKFDFPG RGNTYSSFKW RWYHFDGVDW
210 220 230 240 250
DESRKLSRIY KFRGIGKAWD WEVDTENGNY DYLMYADLDM DHPEVVTELK
260 270 280 290 300
SWGKWYVNTT NIDGFRLDAV KHIKFSFFPD WLSDVRSQTG KPLFTVGEYW
310 320 330 340 350
SYDINKLHNY IMKTNGTMSL FDAPLHNKFY TASKSGGTFD MRTLMTNTLM
360 370 380 390 400
KDQPTLAVTF VDNHDTEPGQ ALQSWVDPWF KPLAYAFILT RQEGYPCVFY
410 420 430 440 450
GDYYGIPQYN IPSLKSKIDP LLIARRDYAY GTQHDYLDHS DIIGWTREGV
460 470 480 490 500
TEKPGSGLAA LITDGPGGSK WMYVGKQHAG KVFYDLTGNR SDTVTINSDG
510 520 530 540
WGEFKVNGGS VSVWVPRKTT VSTIAWSITT RPWTDEFVRW TEPRLVAWP
Length:549
Mass (Da):62,671
Last modified:February 1, 1996 - v3
Checksum:i3A2DD93A955E79D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131M → V in AAA22241 (PubMed:3009417).Curated
Sequence conflicti19 – 191L → W in AAA22241 (PubMed:3009417).Curated
Sequence conflicti23 – 231L → S in CAA26547 (PubMed:3876333).Curated
Sequence conflicti23 – 231L → S in AAA22241 (PubMed:3009417).Curated
Sequence conflicti31 – 311P → H in CAA26547 (PubMed:3876333).Curated
Sequence conflicti31 – 311P → H no nucleotide entry (PubMed:2999073).Curated
Sequence conflicti107 – 1071A → T in CAA26547 (PubMed:3876333).Curated
Sequence conflicti107 – 1071A → T in AAA22241 (PubMed:3009417).Curated
Sequence conflicti167 – 1671T → I in AAA22227 (Ref. 4) Curated
Sequence conflicti179 – 1791P → N in AAA22241 (PubMed:3009417).Curated
Sequence conflicti251 – 2511S → N in CAA26547 (PubMed:3876333).Curated
Sequence conflicti251 – 2511S → N in AAA22241 (PubMed:3009417).Curated
Sequence conflicti260 – 2623TNI → RTL in AAA22227 (Ref. 4) Curated
Sequence conflicti284 – 2841D → Y in CAA26547 (PubMed:3876333).Curated
Sequence conflicti284 – 2841D → Y in AAA22241 (PubMed:3009417).Curated
Sequence conflicti284 – 2841D → Y in AAA22227 (Ref. 4) Curated
Sequence conflicti312 – 3121M → T in CAA26547 (PubMed:3876333).Curated
Sequence conflicti312 – 3121M → T in AAA22241 (PubMed:3009417).Curated
Sequence conflicti338 – 3381T → A in CAA26547 (PubMed:3876333).Curated
Sequence conflicti338 – 3381T → A in AAA22241 (PubMed:3009417).Curated
Sequence conflicti342 – 3421R → S in AAA22241 (PubMed:3009417).Curated
Sequence conflicti346 – 3461T → N in AAA22241 (PubMed:3009417).Curated
Sequence conflicti376 – 3761V → C in CAA26547 (PubMed:3876333).Curated
Sequence conflicti526 – 5272WS → RP in CAA26547 (PubMed:3876333).Curated
Sequence conflicti527 – 5271S → P in AAA22241 (PubMed:3009417).Curated
Sequence conflicti535 – 5351D → G in CAA26547 (PubMed:3876333).Curated
Sequence conflicti535 – 5351D → G in AAA22241 (PubMed:3009417).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11450 Genomic DNA. Translation: AAA22235.2.
X02769 Genomic DNA. Translation: CAA26547.1.
M13255 Genomic DNA. Translation: AAA22241.1.
M57457 Genomic DNA. Translation: AAA22227.1.
PIRiA24436.
A91999. ALBSF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11450 Genomic DNA. Translation: AAA22235.2.
X02769 Genomic DNA. Translation: CAA26547.1.
M13255 Genomic DNA. Translation: AAA22241.1.
M57457 Genomic DNA. Translation: AAA22227.1.
PIRiA24436.
A91999. ALBSF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HVXX-ray2.00A35-549[»]
4UZUX-ray1.90A35-549[»]
ProteinModelPortaliP06279.
SMRiP06279. Positions 35-517.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL5371.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.1. 623.

Miscellaneous databases

EvolutionaryTraceiP06279.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the Bacillus stearothermophilus alpha-amylase gene."
    Nakajima R., Imanaka T., Aiba S.
    J. Bacteriol. 163:401-406(1985) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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], SUBCELLULAR LOCATION.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122, PROTEIN SEQUENCE OF 35-48, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 35-549 IN COMPLEX WITH SODIUM AND CALCIUM, COFACTOR.

Entry informationi

Entry nameiAMY_GEOSE
AccessioniPrimary (citable) accession number: P06279
Secondary accession number(s): Q45519
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.