AMY_GEOSE
ID AMY_GEOSE Reviewed; 549 AA.
AC P06279; Q45519;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1 {ECO:0000269|PubMed:2999073};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=amyS;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 35-39.
RX PubMed=3924897; DOI=10.1128/jb.163.1.401-406.1985;
RA Nakajima R., Imanaka T., Aiba S.;
RT "Nucleotide sequence of the Bacillus stearothermophilus alpha-amylase
RT gene.";
RL J. Bacteriol. 163:401-406(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=DY5/PHI300;
RX PubMed=3876333; DOI=10.1093/oxfordjournals.jbchem.a135279;
RA Ihara H., Sasaki T., Tsuboi A., Yamagata H., Tsukagoshi N., Udaka S.;
RT "Complete nucleotide sequence of a thermophilic alpha-amylase gene:
RT homology between prokaryotic and eukaryotic alpha-amylases at the active
RT sites.";
RL J. Biochem. 98:95-103(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NZ-3;
RX PubMed=3009417; DOI=10.1128/jb.166.2.635-643.1986;
RA Gray G.L., Mainzer S.E., Rey M.W., Lamsa M.H., Kindle K.L., Carmona C.,
RA Requadt C.;
RT "Structural genes encoding the thermophilic alpha-amylases of Bacillus
RT stearothermophilus and Bacillus licheniformis.";
RL J. Bacteriol. 166:635-643(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RA Suominen I., Karp M., Lautamo J., Knowles J., Mantsaelae P.;
RT "Thermostable alpha amylase of Bacillus stearothermophilus: cloning,
RT expression, and secretion by Escherichia coli.";
RL (In) Chaloupka J., Krumphanzl V. (eds.);
RL Extracellular enzymes of microorganisms, pp.129-137, Plenum Press, New York
RL (1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122, PROTEIN SEQUENCE OF 35-48,
RP SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RC STRAIN=DY-5;
RX PubMed=2999073; DOI=10.1128/jb.164.3.1182-1187.1985;
RA Tsukagoshi N., Iritani S., Sasaki T., Takemura T., Ihara H., Idota Y.,
RA Yamagata H., Udaka S.;
RT "Efficient synthesis and secretion of a thermophilic alpha-amylase by
RT protein-producing Bacillus brevis 47 carrying the Bacillus
RT stearothermophilus amylase gene.";
RL J. Bacteriol. 164:1182-1187(1985).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 35-549 IN COMPLEX WITH SODIUM AND
RP CALCIUM, AND COFACTOR.
RX PubMed=11226887; DOI=10.1093/oxfordjournals.jbchem.a002878;
RA Suvd D., Fujimoto Z., Takase K., Matsumura M., Mizuno H.;
RT "Crystal structure of Bacillus stearothermophilus alpha-amylase: possible
RT factors determining the thermostability.";
RL J. Biochem. 129:461-468(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:2999073};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11226887};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:11226887};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11226887};
CC Note=Binds 1 sodium ion per subunit. {ECO:0000269|PubMed:11226887};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2999073,
CC ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M11450; AAA22235.2; -; Genomic_DNA.
DR EMBL; X02769; CAA26547.1; -; Genomic_DNA.
DR EMBL; M13255; AAA22241.1; -; Genomic_DNA.
DR EMBL; M57457; AAA22227.1; -; Genomic_DNA.
DR PIR; A24436; A24436.
DR PIR; A91999; ALBSF.
DR PDB; 1HVX; X-ray; 2.00 A; A=35-549.
DR PDB; 4UZU; X-ray; 1.90 A; A=35-549.
DR PDBsum; 1HVX; -.
DR PDBsum; 4UZU; -.
DR AlphaFoldDB; P06279; -.
DR SMR; P06279; -.
DR ChEMBL; CHEMBL5371; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 3.2.1.1; 623.
DR EvolutionaryTrace; P06279; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR015237; Alpha-amylase_C_pro.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09154; DUF1939; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:2999073,
FT ECO:0000269|PubMed:3924897"
FT CHAIN 35..549
FT /note="Alpha-amylase"
FT /id="PRO_0000001334"
FT ACT_SITE 268
FT /note="Nucleophile"
FT ACT_SITE 298
FT /note="Proton donor"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 196
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 220
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 231
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 237
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 238
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11226887,
FT ECO:0007744|PDB:1HVX"
FT SITE 365
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="M -> V (in Ref. 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="L -> W (in Ref. 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="L -> S (in Ref. 2; CAA26547 and 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="P -> H (in Ref. 2; CAA26547 and 5; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> T (in Ref. 2; CAA26547 and 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="T -> I (in Ref. 4; AAA22227)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="P -> N (in Ref. 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> N (in Ref. 2; CAA26547 and 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..262
FT /note="TNI -> RTL (in Ref. 4; AAA22227)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="D -> Y (in Ref. 2; CAA26547, 3; AAA22241 and 4;
FT AAA22227)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="M -> T (in Ref. 2; CAA26547 and 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="T -> A (in Ref. 2; CAA26547 and 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> S (in Ref. 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="T -> N (in Ref. 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="V -> C (in Ref. 2; CAA26547)"
FT /evidence="ECO:0000305"
FT CONFLICT 526..527
FT /note="WS -> RP (in Ref. 2; CAA26547)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="S -> P (in Ref. 3; AAA22241)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="D -> G (in Ref. 2; CAA26547 and 3; AAA22241)"
FT /evidence="ECO:0000305"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 243..260
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:4UZU"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 415..427
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:4UZU"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:4UZU"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:4UZU"
SQ SEQUENCE 549 AA; 62671 MW; 3A2DD93A955E79D3 CRC64;
MLTFHRIIRK GWMFLLAFLL TALLFCPTGQ PAKAAAPFNG TMMQYFEWYL PDDGTLWTKV
ANEANNLSSL GITALWLPPA YKGTSRSDVG YGVYDLYDLG EFNQKGAVRT KYGTKAQYLQ
AIQAAHAAGM QVYADVVFDH KGGADGTEWV DAVEVNPSDR NQEISGTYQI QAWTKFDFPG
RGNTYSSFKW RWYHFDGVDW DESRKLSRIY KFRGIGKAWD WEVDTENGNY DYLMYADLDM
DHPEVVTELK SWGKWYVNTT NIDGFRLDAV KHIKFSFFPD WLSDVRSQTG KPLFTVGEYW
SYDINKLHNY IMKTNGTMSL FDAPLHNKFY TASKSGGTFD MRTLMTNTLM KDQPTLAVTF
VDNHDTEPGQ ALQSWVDPWF KPLAYAFILT RQEGYPCVFY GDYYGIPQYN IPSLKSKIDP
LLIARRDYAY GTQHDYLDHS DIIGWTREGV TEKPGSGLAA LITDGPGGSK WMYVGKQHAG
KVFYDLTGNR SDTVTINSDG WGEFKVNGGS VSVWVPRKTT VSTIAWSITT RPWTDEFVRW
TEPRLVAWP
