ID AMY_BACSU Reviewed; 659 AA. AC P00691; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 27-MAR-2024, entry version 179. DE RecName: Full=Alpha-amylase; DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P06278}; DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase; DE Flags: Precursor; GN Name=amyE; Synonyms=amyA; OrderedLocusNames=BSU03040; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=6186986; DOI=10.1093/nar/11.2.237; RA Yang M., Galizzi A., Henner D.J.; RT "Nucleotide sequence of the amylase gene from Bacillus subtilis."; RL Nucleic Acids Res. 11:237-249(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=N7 AMYEN+; RX PubMed=6099357; DOI=10.1093/oxfordjournals.jbchem.a135019; RA Yamane K., Hirata Y., Furusato T., Yamazaki H., Nakayama A.; RT "Changes in the properties and molecular weights of Bacillus subtilis M- RT type and N-type alpha-amylases resulting from a spontaneous deletion."; RL J. Biochem. 96:1849-1858(1984). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047; RA Yamane K., Kumano M., Kurita K.; RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: RT determination of the sequence of a 146 kb segment and identification of 113 RT genes."; RL Microbiology 142:3047-3056(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [5] RP SEQUENCE REVISION TO 513-529. RX PubMed=19383706; DOI=10.1099/mic.0.027839-0; RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.; RT "From a consortium sequence to a unified sequence: the Bacillus subtilis RT 168 reference genome a decade later."; RL Microbiology 155:1758-1775(2009). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-557. RX PubMed=6413492; DOI=10.1128/jb.156.1.327-337.1983; RA Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M., RA Tamura G., Yamane K.; RT "Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing RT Bacillus subtilis strain: molecular cloning and nucleotide sequences."; RL J. Bacteriol. 156:327-337(1983). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66. RX PubMed=6189486; DOI=10.1016/0006-291x(83)91516-4; RA Ohmura K., Yamazaki H., Takeichi Y., Nakayama A., Otozai K., Yamane K., RA Yamasaki M., Tamura G.; RT "Nucleotide sequence of the promoter and NH2-terminal signal peptide region RT of Bacillus subtilis alpha-amylase gene cloned in pUB110."; RL Biochem. Biophys. Res. Commun. 112:678-683(1983). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43. RC STRAIN=168 / 2633; RA Emori M., Tojo T., Maruo B.; RT "Molecular cloning and expression of an alpha-amylase gene from an alpha- RT amylase extrahyper producing Bacillus subtilis."; RL Agric. Biol. Chem. 52:399-406(1988). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-58. RX PubMed=112102; DOI=10.1016/s0021-9258(19)86926-0; RA Mantsala P., Zalkin H.; RT "Membrane-bound and soluble extracellular alpha-amylase from Bacillus RT subtilis."; RL J. Biol. Chem. 254:8540-8547(1979). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 42-466 IN COMPLEX WITH CALCIUM RP AND MALTOPENTAOSE, AND COFACTOR. RX PubMed=9514750; DOI=10.1006/jmbi.1997.1599; RA Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T., Mizuno H.; RT "Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus RT subtilis complexed with maltopentaose."; RL J. Mol. Biol. 277:393-407(1998). 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:0000250|UniProtKB:P06278}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:9514750}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:9514750}; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. 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; V00101; CAA23437.1; -; Genomic_DNA. DR EMBL; V00100; CAA23436.1; -; Genomic_DNA. DR EMBL; D50453; BAA08938.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12098.2; -; Genomic_DNA. DR EMBL; K00563; AAA22234.1; -; Genomic_DNA. DR EMBL; X02150; CAA26086.1; -; Genomic_DNA. DR EMBL; M35517; AAA22230.1; -; Genomic_DNA. DR PIR; A00842; ALBS. DR PIR; A91793; ALBSNA. DR RefSeq; NP_388186.2; NC_000964.3. DR RefSeq; WP_003234692.1; NZ_JNCM01000030.1. DR PDB; 1BAG; X-ray; 2.50 A; A=42-466. DR PDB; 1UA7; X-ray; 2.21 A; A=45-466. DR PDBsum; 1BAG; -. DR PDBsum; 1UA7; -. DR AlphaFoldDB; P00691; -. DR SMR; P00691; -. DR STRING; 224308.BSU03040; -. DR BindingDB; P00691; -. DR ChEMBL; CHEMBL3739249; -. DR DrugBank; DB01841; 4,6-Dideoxyglucose. DR DrugBank; DB02120; 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol. DR DrugBank; DB02379; Beta-D-Glucose. DR CAZy; CBM26; Carbohydrate-Binding Module Family 26. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 224308-BSU03040; -. DR EnsemblBacteria; CAB12098; CAB12098; BSU_03040. DR GeneID; 938356; -. DR KEGG; bsu:BSU03040; -. DR PATRIC; fig|224308.179.peg.317; -. DR eggNOG; COG0366; Bacteria. DR InParanoid; P00691; -. DR OrthoDB; 9805159at2; -. DR BioCyc; BSUB:BSU03040-MONOMER; -. DR SABIO-RK; P00691; -. DR EvolutionaryTrace; P00691; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd11315; AmyAc_bac1_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR031965; CBM26. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF16738; CBM26; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; KW Metal-binding; Reference proteome; Secreted; Signal. FT SIGNAL 1..27 FT PROPEP 28..41 FT /id="PRO_0000001335" FT CHAIN 42..659 FT /note="Alpha-amylase" FT /id="PRO_0000001336" FT ACT_SITE 217 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:9514750" FT ACT_SITE 249 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:9514750" FT BINDING 142 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:9514750" FT BINDING 178 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:9514750" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:9514750" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:9514750" FT BINDING 212 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:9514750" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:9514750" FT SITE 310 FT /note="Transition state stabilizer" FT /evidence="ECO:0000305|PubMed:9514750" FT VARIANT 469..477 FT /note="AKAPHVFLE -> EMRCNTFFQ (in strain: N7 AMYEN+)" FT VARIANT 478..659 FT /note="Missing (in strain: N7 AMYEN+)" FT CONFLICT 22 FT /note="H -> Y (in Ref. 2; CAA26086, 6; AAA22234, 7; FT CAA23436 and 8; AAA22230)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="S -> F (in Ref. 2; CAA26086 and 6; AAA22234)" FT /evidence="ECO:0000305" FT CONFLICT 204 FT /note="D -> E (in Ref. 2; CAA26086 and 6; AAA22234)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="N -> K (in Ref. 2; CAA26086)" FT /evidence="ECO:0000305" FT CONFLICT 332 FT /note="A -> S (in Ref. 6; AAA22234)" FT /evidence="ECO:0000305" FT CONFLICT 513..529 FT /note="ETAFKDGDQFTIGKGDP -> DDRRLRMEINSQSEKEIQ (in Ref. 1; FT CAA23437 and 3; BAA08938)" FT /evidence="ECO:0000305" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 60..65 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 67..72 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 96..103 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 105..112 FT /evidence="ECO:0007829|PDB:1UA7" FT TURN 113..115 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 118..129 FT /evidence="ECO:0007829|PDB:1UA7" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:1UA7" FT TURN 148..150 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 153..156 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 174..179 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 193..208 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 234..238 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 258..262 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 270..282 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 294..297 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 309..313 FT /evidence="ECO:0007829|PDB:1UA7" FT TURN 318..321 FT /evidence="ECO:0007829|PDB:1BAG" FT HELIX 324..335 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 337..345 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:1BAG" FT HELIX 369..372 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 374..386 FT /evidence="ECO:0007829|PDB:1UA7" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 402..407 FT /evidence="ECO:0007829|PDB:1UA7" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 411..416 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 418..420 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 432..436 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 438..441 FT /evidence="ECO:0007829|PDB:1BAG" FT STRAND 443..447 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 450..455 FT /evidence="ECO:0007829|PDB:1UA7" FT STRAND 459..463 FT /evidence="ECO:0007829|PDB:1UA7" SQ SEQUENCE 659 AA; 72378 MW; 16BD6CB1E7C67BD6 CRC64; MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG TILHAWNWSF NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY WLYQPTSYQI GNRYLGTEQE FKEMCAAAEE YGIKVIVDAV INHTTSDYAA ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN SLLGLYDWNT QNTQVQSYLK RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN TSAEFQYGEI LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN QIFMNQRGSH GVVLANAGSS SVSINTATKL PDGRYDNKAG AGSFQVNDGK LTGTINARSV AVLYPDDIAK APHVFLENYK TGVTHSFNDQ LTITLRADAN TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG TNSDGVTRTE KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND SGLSGSLPH //