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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Calcium 1Combined sources2 Publications
Metal bindingi190 – 1901Calcium 2Combined sources2 Publications
Metal bindingi190 – 1901Sodium2 Publications
Metal bindingi210 – 2101Calcium 2; via carbonyl oxygenCombined sources2 Publications
Metal bindingi212 – 2121Calcium 2Combined sources2 Publications
Metal bindingi212 – 2121Sodium2 Publications
Metal bindingi223 – 2231Calcium 1Combined sources2 Publications
Metal bindingi223 – 2231Sodium2 Publications
Metal bindingi229 – 2291Calcium 1Combined sources2 Publications
Metal bindingi229 – 2291Sodium2 Publications
Metal bindingi231 – 2311Calcium 2Combined sources2 Publications
Metal bindingi233 – 2331Calcium 2Combined sources2 Publications
Active sitei260 – 2601Nucleophile
Metal bindingi264 – 2641Calcium 1; via carbonyl oxygenCombined sources
Active sitei290 – 2901Proton donor
Metal bindingi329 – 3291Calcium 3; via carbonyl oxygenCombined sources2 Publications
Metal bindingi331 – 3311Calcium 3; via carbonyl oxygenCombined sources2 Publications
Sitei357 – 3571Transition state stabilizerBy similarity
Metal bindingi435 – 4351Calcium 3; via carbonyl oxygenCombined sources2 Publications
Metal bindingi436 – 4361Calcium 3Combined sources2 Publications
Metal bindingi459 – 4591Calcium 3Combined sources2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641H → X: No effect on thermostability. 1 Publication
Mutagenesisi150 – 1501D → X: Decrease in thermostability. 1 Publication
Mutagenesisi155 – 1551N → X: Decrease in thermostability. 1 Publication
Mutagenesisi162 – 1621H → I or V: Increase in thermostability. 1 Publication
Mutagenesisi162 – 1621H → P: Great decrease in thermostability. 1 Publication
Mutagenesisi162 – 1621H → V: Great increase in thermostability; when associated with F-219; V-238; S-293 and Y-294. 1 Publication
Mutagenesisi175 – 1751R → X: No effect on thermostability. 1 Publication
Mutagenesisi193 – 1931D → A, C, E, H or R: Loss of activity. 1 Publication
Mutagenesisi201 – 2011N → H or K: Increase in thermostability. 1 Publication
Mutagenesisi201 – 2011N → R: Great increase in thermostability. 1 Publication
Mutagenesisi207 – 2071Q → X: No effect on thermostability. 1 Publication
Mutagenesisi217 – 2171N → P: Great increase in thermostability. 1 Publication
Mutagenesisi219 – 2191N → A, E, Q, P or S: Great decrease in thermostability. 1 Publication
Mutagenesisi219 – 2191N → F: Great increase in thermostability. Great increase in thermostability; when associated with V-162; V-238; S-293 and Y-294. 1 Publication
Mutagenesisi219 – 2191N → L: Increase in thermostability. 1 Publication
Mutagenesisi221 – 2211N → X: Great decrease in thermostability. 1 Publication
Mutagenesisi229 – 2291D → X: Great decrease in thermostability. 1 Publication
Mutagenesisi233 – 2331D → X: Great decrease in thermostability. 1 Publication
Mutagenesisi238 – 2381A → V: Increase in thermostability. Great increase in thermostability; when associated with V-162; F-219; S-293 and Y-294. 1 Publication
Mutagenesisi276 – 2761H → X: No effect on thermostability. 1 Publication
Mutagenesisi292 – 2921W → L: Decrease in activity; when associated with Y-315. 1 Publication
Mutagenesisi293 – 2931Q → 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 Publication
Mutagenesisi294 – 2941N → 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 Publication
Mutagenesisi298 – 2981A → H, K, L, Q or R: Loss of activity. 1 Publication
Mutagenesisi300 – 3001E → X: No effect on thermostability. 1 Publication
Mutagenesisi315 – 3151V → F: Decrease in activity. 1 Publication
Mutagenesisi315 – 3151V → Y: Increase in activity. Decrease in activity; when associated with W-292. 1 Publication
Mutagenesisi322 – 3221H → X: No effect on thermostability. 1 Publication
Mutagenesisi359 – 3591Q → X: No effect on thermostability. 1 Publication
Mutagenesisi365 – 3651E → H: Loss of activity. 1 Publication
Mutagenesisi435 – 4351H → X: No effect on thermostability. 1 Publication
Mutagenesisi479 – 4791H → X: No effect on thermostability. 1 Publication

Protein family/group databases

Allergomei8255. Bac li aA.

Chemistry

ChEMBLiCHEMBL4215.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 512483Alpha-amylasePRO_0000001332Add
BLAST

Proteomic databases

PRIDEiP06278.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi279010.BLi00656.

Chemistry

BindingDBiP06278.

Structurei

Secondary structure

1
512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Beta strandi46 – 483Combined sources
Helixi50 – 567Combined sources
Helixi58 – 636Combined sources
Beta strandi68 – 703Combined sources
Beta strandi101 – 1033Combined sources
Helixi109 – 12113Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi139 – 14911Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi162 – 1709Combined sources
Turni173 – 1775Combined sources
Helixi186 – 1883Combined sources
Beta strandi189 – 1935Combined sources
Turni196 – 1994Combined sources
Beta strandi204 – 2063Combined sources
Turni207 – 2093Combined sources
Beta strandi213 – 2153Combined sources
Helixi223 – 2264Combined sources
Beta strandi228 – 2303Combined sources
Helixi235 – 25218Combined sources
Beta strandi256 – 2594Combined sources
Helixi262 – 2643Combined sources
Helixi267 – 28115Combined sources
Beta strandi286 – 2894Combined sources
Helixi296 – 30510Combined sources
Turni306 – 3083Combined sources
Beta strandi310 – 3134Combined sources
Helixi315 – 32612Combined sources
Turni327 – 3293Combined sources
Helixi333 – 3375Combined sources
Beta strandi338 – 3403Combined sources
Helixi341 – 3444Combined sources
Helixi346 – 3483Combined sources
Beta strandi349 – 3535Combined sources
Turni356 – 3583Combined sources
Turni370 – 3723Combined sources
Helixi373 – 38210Combined sources
Beta strandi383 – 3864Combined sources
Beta strandi389 – 3913Combined sources
Helixi392 – 3965Combined sources
Beta strandi401 – 4044Combined sources
Helixi410 – 42213Combined sources
Beta strandi428 – 4314Combined sources
Beta strandi434 – 4429Combined sources
Beta strandi453 – 4608Combined sources
Beta strandi463 – 4686Combined sources
Helixi471 – 4733Combined sources
Beta strandi477 – 4804Combined sources
Beta strandi495 – 5017Combined sources
Beta strandi506 – 5105Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 32-512.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41Q → H no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti13 – 131T → P in AAO26743 (PubMed:14632998).Curated
Sequence conflicti13 – 131T → P no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti33 – 331N → I in AAA22232 (PubMed:2265757).Curated
Sequence conflicti38 – 381Q → Y AA sequence (PubMed:6172418).Curated
Sequence conflicti48 – 481G → R no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti62 – 643AEH → VED no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti68 – 692AV → VA no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti72 – 721P → S no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti81 – 811A → D in AAO26743 (PubMed:14632998).Curated
Sequence conflicti81 – 811A → D no nucleotide entry (PubMed:6334606).Curated
Sequence conflicti105 – 11713Missing no nucleotide entry (PubMed:6334606).CuratedAdd
BLAST
Sequence conflicti117 – 1171K → N in AAO26743 (PubMed:14632998).Curated
Sequence conflicti158 – 1581I → T in AAO26743 (PubMed:14632998).Curated
Sequence conflicti162 – 1621H → Q in AAO26743 (PubMed:14632998).Curated
Sequence conflicti163 – 1631R → L in AAA22240 (PubMed:3009417).Curated
Sequence conflicti171 – 1711H → Q in AAO26743 (PubMed:14632998).Curated
Sequence conflicti218 – 2181E → V in AAO26743 (PubMed:14632998).Curated
Sequence conflicti237 – 2382VA → AT in AAO26743 (PubMed:14632998).Curated
Sequence conflicti339 – 3391S → G in AAA22240 (PubMed:3009417).Curated
Sequence conflicti339 – 3391S → G in AAO26743 (PubMed:14632998).Curated
Sequence conflicti347 – 3471L → V in AAO26743 (PubMed:14632998).Curated
Sequence conflicti349 – 3491A → S in AAA22240 (PubMed:3009417).Curated
Sequence conflicti385 – 3851S → A in AAO26743 (PubMed:14632998).Curated
Sequence conflicti390 – 3901V → I in AAO26743 (PubMed:14632998).Curated
Sequence conflicti401 – 4011D → A in AAO26743 (PubMed:14632998).Curated
Sequence conflicti421 – 4211K → I in AAO26743 (PubMed:14632998).Curated
Sequence conflicti464 – 4641A → T in AAO26743 (PubMed:14632998).Curated
Sequence conflicti487 – 4882EP → DS in AAO26743 (PubMed:14632998).Curated
Sequence conflicti493 – 4931S → A in AAO26743 (PubMed:14632998).Curated

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_025807921.1. NZ_JYBQ01000004.1.

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_025807921.1. NZ_JYBQ01000004.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 32-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279010.BLi00656.

Chemistry

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...

Publicationsi

  1. "Complete nucleotide sequence of a gene coding for heat- and pH-stable alpha-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying alpha-amylases deduced from the DNA sequences."
    Yuuki T., Nomura T., Tezuka H., Tsuboi A., Yamagata H., Tsukagoshi N., Udaka S.
    J. Biochem. 98:1147-1156(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 27811 / CCRC 10494 / FERM P-1038.
  2. "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].
  3. "Expression and secretion of an alpha-amylase gene from a native strain of Bacillus licheniformis in Escherichia coli by T7 promoter and putative signal peptide of the gene."
    Shahhoseini M., Ziaee A.A., Ghaemi N.
    J. Appl. Microbiol. 95:1250-1254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  4. "Isolation and the 5'-end nucleotide sequence of Bacillus licheniformis alpha-amylase gene."
    Sibakov M., Palva I.
    Eur. J. Biochem. 145:567-572(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
    Strain: ATCC 14580 / DSM 13 / NBRC 12200 / NCIMB 9375 / NCTC 10341.
  5. "Nucleotide sequence of the 5' region of the Bacillus licheniformis alpha-amylase gene: comparison with the B. amyloliquefaciens gene."
    Stephens M.A., Ortlepp S.A., Ollington J.F., McConnell D.J.
    J. Bacteriol. 158:369-372(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
  6. "In vivo genetic engineering: homologous recombination as a tool for plasmid construction."
    Jorgensen L., Hansen C.K., Poulsen G.B., Diderichsen B.
    Gene 96:37-41(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
  7. "Bacillus licheniformis alpha-amylase gene, amyL, is subject to promoter-independent catabolite repression in Bacillus subtilis."
    Laoide B.M., Chambliss G.H., McConnell D.J.
    J. Bacteriol. 171:2435-2442(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  8. "N-terminal amino acid sequence of Bacillus licheniformis alpha-amylase: comparison with Bacillus amyloliquefaciens and Bacillus subtilis enzymes."
    Kuhn H., Fietzek P.P., Lampen J.O.
    J. Bacteriol. 149:372-373(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-47.
  9. "Action pattern and subsite mapping of Bacillus licheniformis alpha-amylase (BLA) with modified maltooligosaccharide substrates."
    Kandra L., Gyemant G., Remenyik J., Hovanszki G., Liptak A.
    FEBS Lett. 518:79-82(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MAPPING OF SUBSTRATE-BINDING SITE, CATALYTIC ACTIVITY.
  10. "Use of amber suppressors to investigate the thermostability of Bacillus licheniformis alpha-amylase. Amino acid replacements at 6 histidine residues reveal a critical position at His-133."
    Declerck N., Joyet P., Gaillardin C., Masson J.-M.
    J. Biol. Chem. 265:15481-15488(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-64; HIS-162; HIS-276; HIS-322; HIS-435 AND HIS-479.
    Strain: ATCC 6598 / NRS 745.
  11. "Hyperthermostable mutants of Bacillus licheniformis alpha-amylase: multiple amino acid replacements and molecular modelling."
    Declerck N., Joyet P., Trosset J.Y., Garnier J., Gaillardin C.
    Protein Eng. 8:1029-1037(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-238.
    Strain: ATCC 6598 / NRS 745.
  12. "Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase."
    Declerck N., Machius M., Wiegand G., Huber R., Gaillardin C.
    J. Mol. Biol. 301:1041-1057(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-150; ASN-155; ARG-175; ASP-193; ASN-201; GLN-207; ASN-217; ASN-219; ASN-221; ASP-229; ASP-233; ALA-298; GLU-300; GLN-359 AND GLU-365.
    Strain: ATCC 6598 / NRS 745.
  13. "Hyperthermostabilization of Bacillus licheniformis alpha-amylase and modulation of its stability over a 50 degrees C temperature range."
    Declerck N., Machius M., Joyet P., Wiegand G., Huber R., Gaillardin C.
    Protein Eng. 16:287-293(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLN-293 AND ASN-294.
    Strain: ATCC 6598 / NRS 745.
  14. "Alpha-amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity."
    Rivera M.H., Lopez-Munguia A., Soberon X., Saab-Rincon G.
    Protein Eng. 16:505-514(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TRP-292 AND VAL-315.
    Strain: ATCC 27811 / CCRC 10494 / FERM P-1038.
  15. "Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2-A resolution."
    Machius M., Wiegand G., Huber R.
    J. Mol. Biol. 246:545-559(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 30-512.
    Strain: ATCC 27811 / CCRC 10494 / FERM P-1038.
  16. "Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad."
    Machius M., Declerck N., Huber R., Wiegand G.
    Structure 6:281-292(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 30-512 IN COMPLEX WITH CALCIUM AND SODIUM, COFACTOR.
  17. "Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes."
    Brzozowski A.M., Lawson D.M., Turkenburg J.P., Bisgaard-Frantzen H., Svendsen A., Borchert T.V., Dauter Z., Wilson K.S., Davies G.J.
    Biochemistry 39:9099-9107(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 330-512.
  18. "Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface."
    Machius M., Declerck N., Huber R., Wiegand G.
    J. Biol. Chem. 278:11546-11553(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 30-512 OF MUTANT VAL-162/PHE-219/VAL-238/SER-293/TYR-294 IN COMPLEX WITH CALCIUM AND SODIUM, COFACTOR.
    Strain: ATCC 6598 / NRS 745.

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: May 11, 2016
This is version 136 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.