Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi139Calcium 1Combined sources1 Publication1
Metal bindingi196Calcium 2Combined sources1 Publication1
Metal bindingi196SodiumCombined sources1 Publication1
Metal bindingi218Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi220Calcium 2Combined sources1 Publication1
Metal bindingi220SodiumCombined sources1 Publication1
Metal bindingi231Calcium 1Combined sources1 Publication1
Metal bindingi231SodiumCombined sources1 Publication1
Metal bindingi237Calcium 1Combined sources1 Publication1
Metal bindingi237SodiumCombined sources1 Publication1
Metal bindingi238Sodium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi239Calcium 2Combined sources1 Publication1
Active sitei268Nucleophile1
Metal bindingi272Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Active sitei298Proton donor1
Metal bindingi337Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi339Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Sitei365Transition state stabilizerBy similarity1
Metal bindingi440Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi441Calcium 3Combined sources1 Publication1
Metal bindingi464Calcium 3Combined sources1 Publication1

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 databases

ChEMBLiCHEMBL5371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 342 PublicationsAdd BLAST34
ChainiPRO_000000133435 – 549Alpha-amylaseAdd BLAST515

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1549
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 44Combined sources3
Beta strandi52 – 54Combined sources3
Helixi56 – 69Combined sources14
Beta strandi74 – 77Combined sources4
Beta strandi81 – 85Combined sources5
Beta strandi90 – 95Combined sources6
Beta strandi107 – 110Combined sources4
Helixi115 – 127Combined sources13
Beta strandi131 – 136Combined sources6
Beta strandi139 – 141Combined sources3
Beta strandi145 – 156Combined sources12
Beta strandi159 – 163Combined sources5
Beta strandi168 – 176Combined sources9
Turni179 – 183Combined sources5
Helixi192 – 194Combined sources3
Beta strandi195 – 201Combined sources7
Turni202 – 205Combined sources4
Beta strandi206 – 212Combined sources7
Beta strandi234 – 238Combined sources5
Helixi243 – 260Combined sources18
Beta strandi264 – 267Combined sources4
Helixi270 – 272Combined sources3
Helixi277 – 289Combined sources13
Beta strandi294 – 297Combined sources4
Helixi304 – 313Combined sources10
Turni314 – 316Combined sources3
Beta strandi318 – 321Combined sources4
Helixi323 – 333Combined sources11
Turni334 – 337Combined sources4
Helixi341 – 343Combined sources3
Turni344 – 347Combined sources4
Helixi349 – 352Combined sources4
Helixi354 – 356Combined sources3
Beta strandi357 – 361Combined sources5
Turni364 – 366Combined sources3
Turni378 – 380Combined sources3
Helixi381 – 390Combined sources10
Beta strandi391 – 399Combined sources9
Helixi400 – 404Combined sources5
Helixi407 – 409Combined sources3
Helixi415 – 427Combined sources13
Beta strandi433 – 436Combined sources4
Beta strandi439 – 447Combined sources9
Beta strandi458 – 465Combined sources8
Beta strandi468 – 473Combined sources6
Helixi476 – 478Combined sources3
Beta strandi482 – 485Combined sources4
Beta strandi493 – 495Combined sources3
Beta strandi500 – 506Combined sources7
Beta strandi511 – 516Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HVXX-ray2.00A35-549[»]
4UZUX-ray1.90A35-549[»]
ProteinModelPortaliP06279.
SMRiP06279.
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)DescriptionActionsGraphical viewLength
Sequence conflicti13M → V in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti19L → W in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti23L → S in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti23L → S in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti31P → H in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti31P → H no nucleotide entry (PubMed:2999073).Curated1
Sequence conflicti107A → T in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti107A → T in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti167T → I in AAA22227 (Ref. 4) Curated1
Sequence conflicti179P → N in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti251S → N in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti251S → N in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti260 – 262TNI → RTL in AAA22227 (Ref. 4) Curated3
Sequence conflicti284D → Y in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti284D → Y in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti284D → Y in AAA22227 (Ref. 4) Curated1
Sequence conflicti312M → T in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti312M → T in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti338T → A in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti338T → A in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti342R → S in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti346T → N in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti376V → C in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti526 – 527WS → RP in CAA26547 (PubMed:3876333).Curated2
Sequence conflicti527S → P in AAA22241 (PubMed:3009417).Curated1
Sequence conflicti535D → G in CAA26547 (PubMed:3876333).Curated1
Sequence conflicti535D → G in AAA22241 (PubMed:3009417).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HVXX-ray2.00A35-549[»]
4UZUX-ray1.90A35-549[»]
ProteinModelPortaliP06279.
SMRiP06279.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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...

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: November 2, 2016
This is version 121 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.