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Protein

Alpha-amylase

Gene

amyS

Organism
Bacillus licheniformis
Status
Reviewed-Annotation score: Annotation score: 5 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.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • Ca2+2 PublicationsNote: Binds 3 Ca2+ ions per subunit.2 Publications
  • Na+2 PublicationsNote: Binds 1 sodium ion per subunit.2 Publications

pH dependencei

Active up to pH 11.

Temperature dependencei

Active up to 100 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi133Calcium 1Combined sources2 Publications1
Metal bindingi190Calcium 2Combined sources2 Publications1
Metal bindingi190Sodium2 Publications1
Metal bindingi210Calcium 2; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi212Calcium 2Combined sources2 Publications1
Metal bindingi212Sodium2 Publications1
Metal bindingi223Calcium 1Combined sources2 Publications1
Metal bindingi223Sodium2 Publications1
Metal bindingi229Calcium 1Combined sources2 Publications1
Metal bindingi229Sodium2 Publications1
Metal bindingi231Calcium 2Combined sources2 Publications1
Metal bindingi233Calcium 2Combined sources2 Publications1
Active sitei260Nucleophile1
Metal bindingi264Calcium 1; via carbonyl oxygenCombined sources1
Active sitei290Proton donor1
Metal bindingi329Calcium 3; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi331Calcium 3; via carbonyl oxygenCombined sources2 Publications1
Sitei357Transition state stabilizerBy similarity1
Metal bindingi435Calcium 3; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi436Calcium 3Combined sources2 Publications1
Metal bindingi459Calcium 3Combined sources2 Publications1

GO - Molecular functioni

  • alpha-amylase activity Source: CACAO
  • calcium ion binding Source: InterPro

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. 669.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.13 Publications)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
BLA
Gene namesi
Name:amyS
Synonyms:amyL
OrganismiBacillus licheniformis
Taxonomic identifieri1402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Used in the food industry for high temperature liquefaction of starch-containing mashes and in the detergent industry to remove starch. Sold under the name Termamyl by Novozymes.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64H → X: No effect on thermostability. 1 Publication1
Mutagenesisi150D → X: Decrease in thermostability. 1 Publication1
Mutagenesisi155N → X: Decrease in thermostability. 1 Publication1
Mutagenesisi162H → I or V: Increase in thermostability. 1 Publication1
Mutagenesisi162H → P: Great decrease in thermostability. 1 Publication1
Mutagenesisi162H → V: Great increase in thermostability; when associated with F-219; V-238; S-293 and Y-294. 1 Publication1
Mutagenesisi175R → X: No effect on thermostability. 1 Publication1
Mutagenesisi193D → A, C, E, H or R: Loss of activity. 1 Publication1
Mutagenesisi201N → H or K: Increase in thermostability. 1 Publication1
Mutagenesisi201N → R: Great increase in thermostability. 1 Publication1
Mutagenesisi207Q → X: No effect on thermostability. 1 Publication1
Mutagenesisi217N → P: Great increase in thermostability. 1 Publication1
Mutagenesisi219N → A, E, Q, P or S: Great decrease in thermostability. 1 Publication1
Mutagenesisi219N → F: Great increase in thermostability. Great increase in thermostability; when associated with V-162; V-238; S-293 and Y-294. 1 Publication1
Mutagenesisi219N → L: Increase in thermostability. 1 Publication1
Mutagenesisi221N → X: Great decrease in thermostability. 1 Publication1
Mutagenesisi229D → X: Great decrease in thermostability. 1 Publication1
Mutagenesisi233D → X: Great decrease in thermostability. 1 Publication1
Mutagenesisi238A → V: Increase in thermostability. Great increase in thermostability; when associated with V-162; F-219; S-293 and Y-294. 1 Publication1
Mutagenesisi276H → X: No effect on thermostability. 1 Publication1
Mutagenesisi292W → L: Decrease in activity; when associated with Y-315. 1 Publication1
Mutagenesisi293Q → S: Increase in thermostability; when associated with Y-294. Great increase in thermostability; when associated with V-162; F-219; V-238 and Y-294. 1 Publication1
Mutagenesisi294N → Y: Increase in thermostability; when associated with S-293. Great increase in thermostability; when associated with V-162; F-219; V-238 and S-293. 1 Publication1
Mutagenesisi298A → H, K, L, Q or R: Loss of activity. 1 Publication1
Mutagenesisi300E → X: No effect on thermostability. 1 Publication1
Mutagenesisi315V → F: Decrease in activity. 1 Publication1
Mutagenesisi315V → Y: Increase in activity. Decrease in activity; when associated with W-292. 1 Publication1
Mutagenesisi322H → X: No effect on thermostability. 1 Publication1
Mutagenesisi359Q → X: No effect on thermostability. 1 Publication1
Mutagenesisi365E → H: Loss of activity. 1 Publication1
Mutagenesisi435H → X: No effect on thermostability. 1 Publication1
Mutagenesisi479H → X: No effect on thermostability. 1 Publication1

Protein family/group databases

Allergomei8255. Bac li aA.

Chemistry databases

ChEMBLiCHEMBL4215.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000000133230 – 512Alpha-amylaseAdd BLAST483

Proteomic databases

PRIDEiP06278.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi279010.BLi00656.

Chemistry databases

BindingDBiP06278.

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Beta strandi46 – 48Combined sources3
Helixi50 – 56Combined sources7
Helixi58 – 63Combined sources6
Beta strandi68 – 70Combined sources3
Beta strandi101 – 103Combined sources3
Helixi109 – 121Combined sources13
Beta strandi125 – 130Combined sources6
Beta strandi133 – 135Combined sources3
Beta strandi139 – 149Combined sources11
Beta strandi151 – 153Combined sources3
Beta strandi162 – 170Combined sources9
Turni173 – 177Combined sources5
Helixi186 – 188Combined sources3
Beta strandi189 – 193Combined sources5
Turni196 – 199Combined sources4
Beta strandi204 – 206Combined sources3
Turni207 – 209Combined sources3
Beta strandi213 – 215Combined sources3
Helixi223 – 226Combined sources4
Beta strandi228 – 230Combined sources3
Helixi235 – 252Combined sources18
Beta strandi256 – 259Combined sources4
Helixi262 – 264Combined sources3
Helixi267 – 281Combined sources15
Beta strandi286 – 289Combined sources4
Helixi296 – 305Combined sources10
Turni306 – 308Combined sources3
Beta strandi310 – 313Combined sources4
Helixi315 – 326Combined sources12
Turni327 – 329Combined sources3
Helixi333 – 337Combined sources5
Beta strandi338 – 340Combined sources3
Helixi341 – 344Combined sources4
Helixi346 – 348Combined sources3
Beta strandi349 – 353Combined sources5
Turni356 – 358Combined sources3
Turni370 – 372Combined sources3
Helixi373 – 382Combined sources10
Beta strandi383 – 386Combined sources4
Beta strandi389 – 391Combined sources3
Helixi392 – 396Combined sources5
Beta strandi401 – 404Combined sources4
Helixi410 – 422Combined sources13
Beta strandi428 – 431Combined sources4
Beta strandi434 – 442Combined sources9
Beta strandi453 – 460Combined sources8
Beta strandi463 – 468Combined sources6
Helixi471 – 473Combined sources3
Beta strandi477 – 480Combined sources4
Beta strandi495 – 501Combined sources7
Beta strandi506 – 510Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLIX-ray1.90A30-512[»]
1BPLX-ray2.20A30-218[»]
B219-512[»]
1E3XX-ray1.90A330-512[»]
1E3ZX-ray1.93A330-512[»]
1E40X-ray2.20A330-512[»]
1E43X-ray1.70A330-512[»]
1OB0X-ray1.83A30-512[»]
1VJSX-ray1.70A30-512[»]
ProteinModelPortaliP06278.
SMRiP06278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06278.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E5K. Bacteria.
COG0366. LUCA.

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.

P06278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQQKRLYAR LLTLLFALIF LLPHSAAAAA NLNGTLMQYF EWYMPNDGQH
60 70 80 90 100
WKRLQNDSAY LAEHGITAVW IPPAYKGTSQ ADVGYGAYDL YDLGEFHQKG
110 120 130 140 150
TVRTKYGTKG ELQSAIKSLH SRDINVYGDV VINHKGGADA TEDVTAVEVD
160 170 180 190 200
PADRNRVISG EHRIKAWTHF HFPGRGSTYS DFKWHWYHFD GTDWDESRKL
210 220 230 240 250
NRIYKFQGKA WDWEVSNENG NYDYLMYADI DYDHPDVAAE IKRWGTWYAN
260 270 280 290 300
ELQLDGFRLD AVKHIKFSFL RDWVNHVREK TGKEMFTVAE YWQNDLGALE
310 320 330 340 350
NYLNKTNFNH SVFDVPLHYQ FHAASTQGGG YDMRKLLNST VVSKHPLKAV
360 370 380 390 400
TFVDNHDTQP GQSLESTVQT WFKPLAYAFI LTRESGYPQV FYGDMYGTKG
410 420 430 440 450
DSQREIPALK HKIEPILKAR KQYAYGAQHD YFDHHDIVGW TREGDSSVAN
460 470 480 490 500
SGLAALITDG PGGAKRMYVG RQNAGETWHD ITGNRSEPVV INSEGWGEFH
510
VNGGSVSIYV QR
Length:512
Mass (Da):58,549
Last modified:January 1, 1988 - v1
Checksum:iD8BB77759CD4C482
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4Q → H no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti13T → P in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti13T → P no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti33N → I in AAA22232 (PubMed:2265757).Curated1
Sequence conflicti38Q → Y AA sequence (PubMed:6172418).Curated1
Sequence conflicti48G → R no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti62 – 64AEH → VED no nucleotide entry (PubMed:6334606).Curated3
Sequence conflicti68 – 69AV → VA no nucleotide entry (PubMed:6334606).Curated2
Sequence conflicti72P → S no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti81A → D in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti81A → D no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti105 – 117Missing no nucleotide entry (PubMed:6334606).CuratedAdd BLAST13
Sequence conflicti117K → N in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti158I → T in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti162H → Q in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti163R → L in AAA22240 (PubMed:3009417).Curated1
Sequence conflicti171H → Q in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti218E → V in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti237 – 238VA → AT in AAO26743 (PubMed:14632998).Curated2
Sequence conflicti339S → G in AAA22240 (PubMed:3009417).Curated1
Sequence conflicti339S → G in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti347L → V in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti349A → S in AAA22240 (PubMed:3009417).Curated1
Sequence conflicti385S → A in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti390V → I in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti401D → A in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti421K → I in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti464A → T in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti487 – 488EP → DS in AAO26743 (PubMed:14632998).Curated2
Sequence conflicti493S → A in AAO26743 (PubMed:14632998).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03236 Genomic DNA. Translation: CAA26981.1.
M38570 Genomic DNA. Translation: AAA22226.1.
M13256 Genomic DNA. Translation: AAA22240.1.
AF438149 Genomic DNA. Translation: AAO26743.1.
K01984 Genomic DNA. Translation: AAA22193.1.
M62637 Genomic DNA. Translation: AAA22232.1.
M26412 Genomic DNA. Translation: AAA22237.1.
PIRiA91997. ALBSL.
RefSeqiWP_017474613.1. NZ_LQYK01000077.1.
WP_025807921.1. NZ_LYUH01000016.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03236 Genomic DNA. Translation: CAA26981.1.
M38570 Genomic DNA. Translation: AAA22226.1.
M13256 Genomic DNA. Translation: AAA22240.1.
AF438149 Genomic DNA. Translation: AAO26743.1.
K01984 Genomic DNA. Translation: AAA22193.1.
M62637 Genomic DNA. Translation: AAA22232.1.
M26412 Genomic DNA. Translation: AAA22237.1.
PIRiA91997. ALBSL.
RefSeqiWP_017474613.1. NZ_LQYK01000077.1.
WP_025807921.1. NZ_LYUH01000016.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLIX-ray1.90A30-512[»]
1BPLX-ray2.20A30-218[»]
B219-512[»]
1E3XX-ray1.90A330-512[»]
1E3ZX-ray1.93A330-512[»]
1E40X-ray2.20A330-512[»]
1E43X-ray1.70A330-512[»]
1OB0X-ray1.83A30-512[»]
1VJSX-ray1.70A30-512[»]
ProteinModelPortaliP06278.
SMRiP06278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279010.BLi00656.

Chemistry databases

BindingDBiP06278.
ChEMBLiCHEMBL4215.

Protein family/group databases

Allergomei8255. Bac li aA.
CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP06278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105E5K. Bacteria.
COG0366. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.1. 669.

Miscellaneous databases

EvolutionaryTraceiP06278.

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_BACLI
AccessioniPrimary (citable) accession number: P06278
Secondary accession number(s): Q45283, Q84I71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 2, 2016
This is version 139 of the entry and version 1 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.